VSIG1_RAT
ID VSIG1_RAT Reviewed; 404 AA.
AC Q4KLY3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=V-set and immunoglobulin domain-containing protein 1;
DE Flags: Precursor;
GN Name=Vsig1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; BC098943; AAH98943.1; -; mRNA.
DR RefSeq; NP_001032873.1; NM_001037784.1.
DR RefSeq; XP_006234306.1; XM_006234244.3.
DR AlphaFoldDB; Q4KLY3; -.
DR SMR; Q4KLY3; -.
DR STRING; 10116.ENSRNOP00000020974; -.
DR GlyGen; Q4KLY3; 3 sites.
DR iPTMnet; Q4KLY3; -.
DR PhosphoSitePlus; Q4KLY3; -.
DR PaxDb; Q4KLY3; -.
DR Ensembl; ENSRNOT00000082652; ENSRNOP00000075185; ENSRNOG00000054219.
DR GeneID; 315920; -.
DR KEGG; rno:315920; -.
DR CTD; 340547; -.
DR RGD; 1565570; Vsig1.
DR eggNOG; ENOG502QU0R; Eukaryota.
DR GeneTree; ENSGT00940000160507; -.
DR InParanoid; Q4KLY3; -.
DR PRO; PR:Q4KLY3; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000054219; Expressed in stomach and 10 other tissues.
DR ExpressionAtlas; Q4KLY3; baseline.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000920; Myelin_P0-rel.
DR InterPro; IPR029861; VSIG1.
DR PANTHER; PTHR44974; PTHR44974; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR00213; MYELINP0.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..404
FT /note="V-set and immunoglobulin domain-containing protein
FT 1"
FT /id="PRO_0000313575"
FT TOPO_DOM 23..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..133
FT /note="Ig-like V-type"
FT DOMAIN 141..228
FT /note="Ig-like C2-type"
FT REGION 266..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..343
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2J4"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 404 AA; 43938 MW; F24F85AAD66E36FD CRC64;
MMVFAFWKVF LILNCLAGQV NMVQVTIPDT FVNVTVGSNV TLLCLYTTTV TSLEKLSIQW
SFFHNKEMEP ISIYYSEGGQ ASAIGQFKDR IIGATNPGNA SITILHMQPA DSGIYICDVN
NPPDFFGKNQ GILDVTVLVK PSKPFCSIQG RPEAGHPISL SCLSAFGTPS PVYYWYKIEG
NTIVPVKESF NSATGVLDIG NLTNFEKGYY QCTAINSLGN SSCEIDLTSS DPEVGIIIGA
LVGALTGAAI IICVVYFARN KVKSKQKNLN SSTELEPMTK VHHSRQNEAI PAGGIQLEGT
LPSSIHASHN TEPTTAVLEP EYEPNPPLET ATQPDPEPEG SGPMPVPETE IQLQPEMELE
PETEPEPEPE PEPQPELESE LEPDPQSGVI VEPMREEEKE TVKA
