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VSIG2_MOUSE
ID   VSIG2_MOUSE             Reviewed;         328 AA.
AC   Q9Z109; Q9CVA4; Q9D0T4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=V-set and immunoglobulin domain-containing protein 2;
DE   AltName: Full=Cortical thymocyte-like protein;
DE            Short=CT-like protein;
DE   Flags: Precursor;
GN   Name=Vsig2; Synonyms=Ctm, Ctxl;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=9862345;
RX   DOI=10.1002/(sici)1521-4141(199812)28:12<4094::aid-immu4094>3.0.co;2-2;
RA   Chretien I., Marcuz A., Courtet M., Katevuo K., Vainio O., Heath J.K.,
RA   White S.J., Du Pasquier L.;
RT   "CTX, a Xenopus thymocyte receptor, defines a molecular family conserved
RT   throughout vertebrates.";
RL   Eur. J. Immunol. 28:4094-4104(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-304 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Stomach;
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).
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=Q9Z109-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z109-2; Sequence=VSP_014120;
CC   -!- TISSUE SPECIFICITY: Expressed in the stomach, colon and prostate.
CC       {ECO:0000269|PubMed:9862345}.
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DR   EMBL; AF061024; AAD17524.1; -; Genomic_DNA.
DR   EMBL; AK004478; BAB23323.1; -; mRNA.
DR   EMBL; AK008920; BAB25968.1; -; mRNA.
DR   CCDS; CCDS22980.1; -. [Q9Z109-1]
DR   RefSeq; NP_065264.2; NM_020518.2. [Q9Z109-1]
DR   AlphaFoldDB; Q9Z109; -.
DR   SMR; Q9Z109; -.
DR   STRING; 10090.ENSMUSP00000002008; -.
DR   GlyGen; Q9Z109; 3 sites.
DR   PhosphoSitePlus; Q9Z109; -.
DR   MaxQB; Q9Z109; -.
DR   PaxDb; Q9Z109; -.
DR   PRIDE; Q9Z109; -.
DR   ProteomicsDB; 275192; -. [Q9Z109-1]
DR   ProteomicsDB; 275193; -. [Q9Z109-2]
DR   Antibodypedia; 32904; 250 antibodies from 24 providers.
DR   DNASU; 57276; -.
DR   Ensembl; ENSMUST00000002008; ENSMUSP00000002008; ENSMUSG00000001943. [Q9Z109-1]
DR   Ensembl; ENSMUST00000215271; ENSMUSP00000150115; ENSMUSG00000001943. [Q9Z109-2]
DR   GeneID; 57276; -.
DR   KEGG; mmu:57276; -.
DR   UCSC; uc009ovb.1; mouse. [Q9Z109-1]
DR   UCSC; uc012gra.1; mouse. [Q9Z109-2]
DR   CTD; 23584; -.
DR   MGI; MGI:1928009; Vsig2.
DR   VEuPathDB; HostDB:ENSMUSG00000001943; -.
DR   eggNOG; ENOG502RYI3; Eukaryota.
DR   GeneTree; ENSGT00940000161544; -.
DR   HOGENOM; CLU_040549_1_0_1; -.
DR   InParanoid; Q9Z109; -.
DR   OMA; TPKETYG; -.
DR   OrthoDB; 841952at2759; -.
DR   PhylomeDB; Q9Z109; -.
DR   TreeFam; TF330875; -.
DR   BioGRID-ORCS; 57276; 2 hits in 71 CRISPR screens.
DR   PRO; PR:Q9Z109; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9Z109; protein.
DR   Bgee; ENSMUSG00000001943; Expressed in pyloric antrum and 71 other tissues.
DR   ExpressionAtlas; Q9Z109; baseline and differential.
DR   Genevisible; Q9Z109; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISA: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; IPR042475; VSIG2.
DR   PANTHER; PTHR45046; PTHR45046; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..328
FT                   /note="V-set and immunoglobulin domain-containing protein
FT                   2"
FT                   /id="PRO_0000015005"
FT   TOPO_DOM        25..244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..328
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..138
FT                   /note="Ig-like V-type"
FT   DOMAIN          145..234
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        167..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         22..101
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014120"
FT   CONFLICT        158
FT                   /note="S -> L (in Ref. 1; AAD17524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="G -> C (in Ref. 1; AAD17524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="N -> H (in Ref. 1; AAD17524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="E -> D (in Ref. 1; AAD17524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269..274
FT                   /note="KERKKE -> TEGTGA (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="K -> R (in Ref. 1; BAB23323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="Q -> P (in Ref. 1; AAD17524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="T -> A (in Ref. 1; AAD17524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="T -> P (in Ref. 1; AAD17524)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  34514 MW;  C57A121CC64E9617 CRC64;
     MAWPLVGAFL CGHLLGFVCL SGLAVEVTVP TEPLSVPKGK TAELSCSYKT SVGDNFALEW
     SFVQPGKPIS ASVPVLYFTN GHLYPTGSKA DRAILLHDPP TGGLATLKLT DLRPSDTGTY
     LCNVNNPPDF YTNGLGLINL TVLVPPSHPL CSQSGQTSVG GSAALGCRSS EGAPKPVYNW
     ERLGSSPTPP PGSMVQDEVS GQLILTNLSL TSSGTYRCVA SNQMGSASCE LNLSVTDSSE
     GRVAGTLIGV LLGVLLLSVA AFCLIRFQKE RKKEPKETYG GSDLREDATA PGVFEQASMR
     ADHSKELLEK SPCASTMTTT KSKLSMVV
 
 
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