8S9P


Conserved Protein Domain Family
NtA
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pfam03146: NtA (This model is not part of the current CDD release)
Agrin NtA domain
Agrin is a multidomain heparan sulphate proteoglycan, that is a key organiser for the induction of postsynaptic specialisations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The structure of this domain is an OB-fold.
Links
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Statistics
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PSSM-Id: 515411
Aligned: 4 rows
Threshold Bit Score: 139.65
Created: 13-Feb-2025
Updated: 28-Apr-2025
Structure
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Program:
Drawing:
Aligned Rows:
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PubMed ReferencesClick to see Conserved Features Help
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
8S9P_A         31 CPERALERREEEANVVLTGTVEEILNvDPVQHTYSCKVRVWRYLKGKDLVAresl-------ldgGNKV-VIS--GFGDP 100  human
XP_015785065   42 CRDKVPRKLTDLSNVVLTGFIEQTYPsLDNGEIYSGSVLVKRVFRGPSKFQ--------------GNRV-TID--GLGDA 104 
XP_009027575   36 CFDLTIEEKVNNAEFIFSGTVREVRY-NVDKKAQKASVEIKRIFKGQHKLTqlflseikgrflpiVHKVcTVE--GLGLD 112 
XP_026691460   62 CLDRTTTEKNSTSTVILTGTVQYCDViRAGS--YKCNIKIWRVMKGNSLAMnlitiqkqgiltsmYKKK-YVDvyGLGNS 138  vase tunicate

8S9P_A        101 LICDNQVSTGDTRIFFVNPAPP-YlwpahkneLMLNSSLMRITLRNL 146  human
XP_015785065  105 SYCQSKGQRGESWIFQLSQISDgY--------FRLNGTLLKLNLDNL 143 
XP_009027575  113 GLCSSHTRVFDTWLFFTNPVDD-K--------LQLNSSLVRLSVMSI 150 
XP_026691460  139 AFCKSNVERADTRIFFLNKLNN-R--------LVVSASLDRITLKNL 176  vase tunicate
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