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    SPTAN1 spectrin alpha, non-erythrocytic 1 [ Gallus gallus (chicken) ]

    Gene ID: 374234, updated on 3-Apr-2024

    Summary

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    Symbol
    SPTAN1provided by CGNC
    Full Name
    spectrin alpha, non-erythrocytic 1provided by CGNC
    Primary source
    CGNC:3498
    See related
    Ensembl:ENSGALG00010028556
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Gallus gallus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; Phasianinae; Gallus
    Also known as
    SPECA
    Orthologs
    human mouse all
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    Genomic context

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    Location:
    chromosome: 17
    Exon count:
    62
    Annotation release Status Assembly Chr Location
    106 current bGalGal1.mat.broiler.GRCg7b (GCF_016699485.2) 17 NC_052548.1 (5815166..5861030)
    106 current bGalGal1.pat.whiteleghornlayer.GRCg7w (GCF_016700215.2) 17 NC_052589.1 (5229136..5275008)

    Chromosome 17 - NC_052548.1Genomic Context describing neighboring genes Neighboring gene outer dense fiber of sperm tails 2 Neighboring gene GLE1, RNA export mediator Neighboring gene uncharacterized LOC107052167 Neighboring gene WD repeat domain 34 Neighboring gene uncharacterized LOC112529986 Neighboring gene SET nuclear proto-oncogene

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Protein Motional Details Revealed by Complementary Structural Biology Techniques. Grohe K, et al. Structure, 2020 Sep 1. PMID 32579946
    2. Non-equilibrium hydrogen exchange for determination of H-bond strength and water accessibility in solid proteins. Grohe K, et al. J Biomol NMR, 2017 May. PMID 28393279
    3. Thermal stability of chicken brain α-spectrin repeat 17: a spectroscopic study. Brenner AK, et al. J Biomol NMR, 2012 Jun. PMID 22569754
    4. Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanisms. Wensley BG, et al. J Mol Biol, 2009 Jul 31. PMID 19445951, Free PMC Article
    5. The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3. Casares S, et al. BMC Struct Biol, 2007 Apr 2. PMID 17407569, Free PMC Article

    See all (21) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Protein Motional Details Revealed by Complementary Structural Biology Techniques.
      Title: Protein Motional Details Revealed by Complementary Structural Biology Techniques.
    2. Tracking of the NMR HN peak intensities for 2 weeks reports on site-specific hydrogen bond strength and also likely reflects water accessibility in a qualitative manner.
      Title: Non-equilibrium hydrogen exchange for determination of H-bond strength and water accessibility in solid proteins.
    3. Spectroscopic study of the thermal stability of chicken brain alpha-spectrin repeat 17.
      Title: Thermal stability of chicken brain α-spectrin repeat 17: a spectroscopic study.
    4. The rate-limiting transition state for R15 folding is investigated using protein engineering methods (Phi-value analysis) and compared with previously completed analyses of R16 and R17 (15th, 16th repeats of alpha-spectrin).
      Title: Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanisms.
    5. Spectrin-titin domain pairs of both spectrin R16 and R17 with a single titin I27 domain at either the N- or the C-terminus were created and found that spectrin domains are significantly stabilized, by nonnative interactions at the C-terminus only.
      Title: Distinguishing specific and nonspecific interdomain interactions in multidomain proteins.
    6. protein engineering phi-value analysis of the 16th domain of brain alpha-spectrin
      Title: The folding of spectrin domains II: phi-value analysis of R16.
    7. kinetic characterisation of the wild-type forms of the 15th, 16th, and 17th domains of brain alpha-spectrin
      Title: The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties.
    8. Data show that mutation of alpha-spectrin asparagine 47 to alanine induces the formation of amyloid fibrils under mild acid conditions.
      Title: A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.
    9. The high-resolution structure of the complex between the R21A mutant of Spc-SH3 and p41 derived from nuclear magnetic resonance data, is presented.
      Title: The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3.
    10. Results describe the folding pathway of the 17th domain of chicken brain alpha-spectrin, R17.
      Title: The folding pathway of spectrin R17 from experiment and simulation: using experimentally validated MD simulations to characterize States hinted at by experiment.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables actin filament binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    enables calcium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in actin cytoskeleton organization IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cell junction IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    located_in cell projection IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    located_in cortical actin cytoskeleton IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    spectrin alpha chain, non-erythrocytic 1
    Names
    alpha-II spectrin
    alpha-spectrin
    fodrin alpha chain
    nonerythroid alpha-spectrin
    spectrin alpha chain, brain
    spectrin, alpha, non-erythrocytic 1 (alpha-fodrin)
    spectrin, non-erythroid alpha chain

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001042538.2 → NP_001036003.2  spectrin alpha chain, non-erythrocytic 1

      Status: PROVISIONAL

      Source sequence(s)
      JAENSK010000308
      UniProtKB/TrEMBL
      A0A8V1AEP9
      Related
      ENSGALP00010042613.1, ENSGALT00010069171.1
      Conserved Domains (4) summary
      smart00150
      Location:49 → 145
      SPEC; Spectrin repeats
      cd11808
      Location:971 → 1023
      SH3_Alpha_Spectrin; Src homology 3 domain of Alpha Spectrin
      cd00051
      Location:2332 → 2400
      EFh; EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to ...
      cd00176
      Location:679 → 890
      SPEC; Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; ...

    RefSeqs of Annotated Genomes: Gallus gallus Annotation Release 106 details...Open this link in a new tab

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference bGalGal1.mat.broiler.GRCg7b Primary Assembly

    Genomic

    1. NC_052548.1 Reference bGalGal1.mat.broiler.GRCg7b Primary Assembly

      Range
      5815166..5861030
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_046901619.1 → XP_046757575.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    2. XM_046901623.1 → XP_046757579.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

      Related
      ENSGALP00010042618.1, ENSGALT00010069176.1

    3. XM_046901627.1 → XP_046757583.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    4. XM_046901621.1 → XP_046757577.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    5. XM_046901634.1 → XP_046757590.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    6. XM_046901624.1 → XP_046757580.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    7. XM_046901629.1 → XP_046757585.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    8. XM_046901622.1 → XP_046757578.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    9. XM_046901633.1 → XP_046757589.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    10. XM_046901625.1 → XP_046757581.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    11. XM_046901631.1 → XP_046757587.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    12. XM_046901632.1 → XP_046757588.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    13. XM_046901626.1 → XP_046757582.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    14. XM_046901628.1 → XP_046757584.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    15. XM_046901620.1 → XP_046757576.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    16. XM_046901630.1 → XP_046757586.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    17. XM_040648916.2 → XP_040504850.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

      UniProtKB/TrEMBL
      A0A8V1AH25
      Related
      ENSGALP00010042615.1, ENSGALT00010069173.1
      Conserved Domains (5) summary
      cd11808
      Location:983 → 1035
      SH3_Alpha_Spectrin; Src homology 3 domain of Alpha Spectrin
      cd00051
      Location:2365 → 2433
      EFh; EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to ...
      cd00176
      Location:691 → 902
      SPEC; Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; ...
      pfam00435
      Location:1675 → 1779
      Spectrin; Spectrin repeat
      pfam08726
      Location:2440 → 2508
      EFhand_Ca_insen; Ca2+ insensitive EF hand

    18. XM_015279289.4 → XP_015134775.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

      UniProtKB/TrEMBL
      A0A8V1AH25
      Conserved Domains (5) summary
      cd11808
      Location:971 → 1023
      SH3_Alpha_Spectrin; Src homology 3 domain of Alpha Spectrin
      cd00051
      Location:2353 → 2421
      EFh; EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to ...
      cd00176
      Location:679 → 890
      SPEC; Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; ...
      pfam00435
      Location:1663 → 1767
      Spectrin; Spectrin repeat
      pfam08726
      Location:2428 → 2496
      EFhand_Ca_insen; Ca2+ insensitive EF hand

    Alternate bGalGal1.pat.whiteleghornlayer.GRCg7w

    Genomic

    1. NC_052589.1 Alternate bGalGal1.pat.whiteleghornlayer.GRCg7w

      Range
      5229136..5275008
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_046928669.1 → XP_046784625.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    2. XM_046928674.1 → XP_046784630.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    3. XM_046928679.1 → XP_046784635.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    4. XM_046928671.1 → XP_046784627.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    5. XM_046928686.1 → XP_046784642.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    6. XM_046928675.1 → XP_046784631.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    7. XM_046928681.1 → XP_046784637.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    8. XM_046928672.1 → XP_046784628.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    9. XM_046928685.1 → XP_046784641.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    10. XM_046928676.1 → XP_046784632.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    11. XM_046928683.1 → XP_046784639.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    12. XM_046928684.1 → XP_046784640.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    13. XM_046928677.1 → XP_046784633.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    14. XM_046928680.1 → XP_046784636.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    15. XM_046928670.1 → XP_046784626.1  spectrin alpha chain, non-erythrocytic 1 isoform X1

    16. XM_046928682.1 → XP_046784638.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    17. XM_046928673.1 → XP_046784629.1  spectrin alpha chain, non-erythrocytic 1 isoform X2

    18. XM_046928678.1 → XP_046784634.1  spectrin alpha chain, non-erythrocytic 1 isoform X3

    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P07751.3 GenPept UniProtKB/Swiss-Prot:P07751

    Gene LinkOut

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