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VSIG1_MOUSE
ID   VSIG1_MOUSE             Reviewed;         407 AA.
AC   Q9D2J4; Q9D9J0; Q9DA22;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=V-set and immunoglobulin domain-containing protein 1;
DE   AltName: Full=Cell surface A33 antigen;
DE   AltName: Full=Glycoprotein A34;
DE   Flags: Precursor;
GN   Name=Vsig1; Synonyms=Gpa34;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=16405301;
RA   Scanlan M.J., Ritter G., Yin B.W., Williams C. Jr., Cohen L.S.,
RA   Coplan K.A., Fortunato S.R., Frosina D., Lee S.Y., Murray A.E., Chua R.,
RA   Filonenko V.V., Sato E., Old L.J., Jungbluth A.A.;
RT   "Glycoprotein A34, a novel target for antibody-based cancer
RT   immunotherapy.";
RL   Cancer Immun. 6:2-2(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-274, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D2J4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D2J4-2; Sequence=VSP_030028;
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DR   EMBL; DQ007336; AAY56125.1; -; mRNA.
DR   EMBL; AK006251; BAB24483.1; -; mRNA.
DR   EMBL; AK006862; BAB24769.1; -; mRNA.
DR   EMBL; AK019565; BAB31795.1; -; mRNA.
DR   CCDS; CCDS30443.1; -. [Q9D2J4-1]
DR   RefSeq; NP_080379.1; NM_026103.1.
DR   AlphaFoldDB; Q9D2J4; -.
DR   SMR; Q9D2J4; -.
DR   STRING; 10090.ENSMUSP00000033806; -.
DR   GlyGen; Q9D2J4; 3 sites.
DR   iPTMnet; Q9D2J4; -.
DR   PhosphoSitePlus; Q9D2J4; -.
DR   MaxQB; Q9D2J4; -.
DR   PaxDb; Q9D2J4; -.
DR   PRIDE; Q9D2J4; -.
DR   ProteomicsDB; 297590; -. [Q9D2J4-1]
DR   ProteomicsDB; 297591; -. [Q9D2J4-2]
DR   ABCD; Q9D2J4; 44 sequenced antibodies.
DR   DNASU; 78789; -.
DR   GeneID; 78789; -.
DR   KEGG; mmu:78789; -.
DR   CTD; 340547; -.
DR   MGI; MGI:1926039; Vsig1.
DR   eggNOG; ENOG502QU0R; Eukaryota.
DR   InParanoid; Q9D2J4; -.
DR   BioGRID-ORCS; 78789; 1 hit in 74 CRISPR screens.
DR   PRO; PR:Q9D2J4; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9D2J4; protein.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:MGI.
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   Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..407
FT                   /note="V-set and immunoglobulin domain-containing protein
FT                   1"
FT                   /id="PRO_0000313574"
FT   TOPO_DOM        23..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..134
FT                   /note="Ig-like V-type"
FT   DOMAIN          145..229
FT                   /note="Ig-like C2-type"
FT   REGION          268..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        44..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        163..213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..107
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030028"
FT   CONFLICT        125
FT                   /note="H -> D (in Ref. 2; BAB24483/BAB24769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="N -> K (in Ref. 2; BAB24483/BAB24769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="S -> T (in Ref. 2; BAB24483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="E -> K (in Ref. 2; BAB24769)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  44015 MW;  B7094F818B868680 CRC64;
     MMVFAFWKVF LILNCLAGQV SMVQVTIPDT FVNVTVGSNV TLLCLYTTTE KSLEKLSIQW
     SFFHNKEMEE PISIYYSEGG QASAIGQFKD RIIGATNPGN ASITILHMQP ADSGIYICDV
     NNPPHFVGKN QGLLDVTVLV KPSKPFCTIQ GRPEAGHPIS LSCLSAFGTP SPLYYWYNIE
     GNTIVPVKES FNTATGVLVI GNLTNFEQGY YQCTAINSLG NSSCEIDLTS SHPEVGIIIG
     ALVGALIGAA VIICVVYFAR NKVKSKQQKN LNSSTELEPM TKVHHPQQSE AISADGVQLE
     GTLPSSIHAG HNTEPTTTAV LEPEYEPNPP LETTTQPDPE PEGSVPVLAP EAEIQPHPEL
     DPETETEPEP EPEPKPEPEP EPELEPDPQS GVIIEPLSKA GEDTVKA
 
 
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