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The following sections contain reference sequences that belong to a
specific genome build. Explain
This section includes genomic Reference
Sequences (RefSeqs) from all assemblies on which this gene is annotated, such as
RefSeqs for chromosomes and scaffolds (contigs) from both reference and alternate
assemblies. Model RNAs and proteins are also reported here.
Reference NHGRI_mPanTro3-v2.0_pri Primary Assembly
Genomic
-
NC_072419.2 Reference NHGRI_mPanTro3-v2.0_pri Primary Assembly
- Range
-
57891758..58063793 complement
- Download
- GenBank, FASTA, Sequence Viewer (Graphics)
mRNA and Protein(s)
-
XM_024352113.3 → XP_024207881.1 probable phospholipid-transporting ATPase IIA isoform X1
- UniProtKB/TrEMBL
- A0A2I3TTY5, A0A2J8MJ87, A0A8I3B2E1, K7D8N5, K7DK45
- Conserved Domains (2) summary
-
- cd07541
Location:55 → 967
- P-type_ATPase_APLT_Neo1-like; Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B
- pfam13246
Location:464 → 571
- Cation_ATPase; Cation transport ATPase (P-type)
-
XM_009437420.5 → XP_009435695.1 probable phospholipid-transporting ATPase IIA isoform X2
See identical proteins and their annotated locations for XP_009435695.1
- UniProtKB/TrEMBL
- A0A2I3SFP0, H2QKK9
- Related
-
ENSPTRP00000075795.1
- Conserved Domains (6) summary
-
- cd01427
Location:630 → 780
- HAD_like; Haloacid dehalogenase-like hydrolases. The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others, ...
- TIGR01652
Location:31 → 1023
- ATPase-Plipid; phospholipid-translocating P-type ATPase, flippase
- pfam00122
Location:119 → 315
- E1-E2_ATPase; E1-E2 ATPase
- pfam13246
Location:477 → 551
- Cation_ATPase; Cation transport ATPase (P-type)
- pfam16209
Location:18 → 82
- PhoLip_ATPase_N; Phospholipid-translocating ATPase N-terminal
- pfam16212
Location:789 → 1017
- PhoLip_ATPase_C; Phospholipid-translocating P-type ATPase C-terminal