ID A0A1S3GRJ0_DIPOR Unreviewed; 249 AA.
AC A0A1S3GRJ0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Vesicle-associated membrane protein-associated protein A {ECO:0000256|ARBA:ARBA00018309};
GN Name=Vapa {ECO:0000313|RefSeq:XP_012891300.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012891300.1};
RN [1] {ECO:0000313|RefSeq:XP_012891300.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012891300.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004521}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004521}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000256|ARBA:ARBA00008932}.
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DR RefSeq; XP_012891300.1; XM_013035846.1.
DR AlphaFoldDB; A0A1S3GRJ0; -.
DR STRING; 10020.ENSDORP00000020857; -.
DR GeneID; 106000570; -.
DR KEGG; dord:106000570; -.
DR CTD; 9218; -.
DR OMA; CVFENPV; -.
DR OrthoDB; 122649at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0033149; F:FFAT motif binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0035627; P:ceramide transport; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IEA:Ensembl.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:Ensembl.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0015914; P:phospholipid transport; IEA:Ensembl.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IEA:Ensembl.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IEA:Ensembl.
DR GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR016763; VAP.
DR PANTHER; PTHR10809; VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR10809:SF155; VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN A; 1.
DR Pfam; PF00635; Motile_Sperm; 1.
DR PIRSF; PIRSF019693; VAMP-associated; 1.
DR SUPFAM; SSF49354; PapD-like; 1.
DR PROSITE; PS50202; MSP; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..131
FT /note="MSP"
FT /evidence="ECO:0000259|PROSITE:PS50202"
FT REGION 135..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..199
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 249 AA; 27965 MW; D3118F7E02908E99 CRC64;
MASASGAMAK YEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK VKTTAPRRYC
VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNFTDME AVWKEAKPDE
LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPMP KPHSASLNDT ETRKLMEECK
RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSTATF RDNVTSPLPS LLVVIAAIFI
GFFLGKFIL
//
