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CEA20_MOUSE
ID   CEA20_MOUSE             Reviewed;         577 AA.
AC   Q9D2Z1; Q80Y42;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 20 {ECO:0000303|PubMed:16139472};
DE   Flags: Precursor;
GN   Name=Ceacam20 {ECO:0000303|PubMed:16139472};
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 {ECO:0000312|Proteomes:UP000000589};
RN   [1] {ECO:0000312|EMBL:BAB31307.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum {ECO:0000312|EMBL:BAB31307.1};
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   [2] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000312|EMBL:AAH49361.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000312|EMBL:AAH49361.1};
RC   TISSUE=Colon {ECO:0000312|EMBL:AAH49361.1};
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   [4] {ECO:0000305}
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=16139472; DOI=10.1016/j.ygeno.2005.07.008;
RA   Zebhauser R., Kammerer R., Eisenried A., McLellan A., Moore T.,
RA   Zimmermann W.;
RT   "Identification of a novel group of evolutionarily conserved members within
RT   the rapidly diverging murine Cea family.";
RL   Genomics 86:566-580(2005).
RN   [5] {ECO:0000305}
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=25908210; DOI=10.1111/gtc.12247;
RA   Kitamura Y., Murata Y., Park J.H., Kotani T., Imada S., Saito Y.,
RA   Okazawa H., Azuma T., Matozaki T.;
RT   "Regulation by gut commensal bacteria of carcinoembryonic antigen-related
RT   cell adhesion molecule expression in the intestinal epithelium.";
RL   Genes Cells 20:578-589(2015).
RN   [6] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH PTPRH AND SYK, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, PHOSPHORYLATION AT TYR-559 AND TYR-570, MUTAGENESIS OF TYR-559
RP   AND TYR-570, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=26195794; DOI=10.1073/pnas.1510167112;
RA   Murata Y., Kotani T., Supriatna Y., Kitamura Y., Imada S., Kawahara K.,
RA   Nishio M., Daniwijaya E.W., Sadakata H., Kusakari S., Mori M., Kanazawa Y.,
RA   Saito Y., Okawa K., Takeda-Morishita M., Okazawa H., Ohnishi H., Azuma T.,
RA   Suzuki A., Matozaki T.;
RT   "Protein tyrosine phosphatase SAP-1 protects against colitis through
RT   regulation of CEACAM20 in the intestinal epithelium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E4264-E4271(2015).
CC   -!- FUNCTION: Together with the tyrosine-protein kinase SYK, enhances
CC       production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus
CC       have a role in the intestinal immune response.
CC       {ECO:0000269|PubMed:26195794}.
CC   -!- SUBUNIT: Interacts (via extracellular domain) with PTPRH (via
CC       extracellular domain); the interaction dephosphorylates CEACAM20.
CC       Interacts (phosphorylated form) with SYK (via SH2 domains); the
CC       interaction further enhances CEACAM20 phosphorylation.
CC       {ECO:0000269|PubMed:26195794}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
CC       {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}; Single-pass
CC       type I membrane protein {ECO:0000305}. Apical cell membrane
CC       {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}; Single-pass
CC       type I membrane protein {ECO:0000305}. Note=Colocalizes with PTPRH and
CC       CEACAM1 at the apical brush border of intestinal cells.
CC       {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in the small intestine and colon
CC       (at protein level) (PubMed:25908210, PubMed:26195794). Minimal
CC       expression in other tissues (at protein level) (PubMed:26195794).
CC       Highly expressed in cecum, colon, ileum, jejunum, and testis, and also
CC       detected at lower levels in salivary gland and thymus
CC       (PubMed:16139472). {ECO:0000269|PubMed:16139472,
CC       ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}.
CC   -!- INDUCTION: In intestinal epithelium, up-regulated in the presence of
CC       Gram-positive commensal gut bacteria. May also be up-regulated by
CC       interferon gamma (IFNG) and butyrate (a product of bacterial
CC       fermentation). {ECO:0000269|PubMed:25908210}.
CC   -!- PTM: Phosphorylated on tyrosine residues by SYK, SRC and FYN in vitro.
CC       {ECO:0000269|PubMed:26195794}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC       {ECO:0000305}.
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DR   EMBL; AK018613; BAB31307.1; -; mRNA.
DR   EMBL; AC130530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC049361; AAH49361.1; -; mRNA.
DR   CCDS; CCDS20919.1; -.
DR   RefSeq; NP_082115.2; NM_027839.2.
DR   AlphaFoldDB; Q9D2Z1; -.
DR   SMR; Q9D2Z1; -.
DR   STRING; 10090.ENSMUSP00000092344; -.
DR   GlyGen; Q9D2Z1; 3 sites.
DR   iPTMnet; Q9D2Z1; -.
DR   PhosphoSitePlus; Q9D2Z1; -.
DR   PaxDb; Q9D2Z1; -.
DR   PRIDE; Q9D2Z1; -.
DR   ProteomicsDB; 281167; -.
DR   Antibodypedia; 72273; 21 antibodies from 9 providers.
DR   DNASU; 71601; -.
DR   Ensembl; ENSMUST00000094753; ENSMUSP00000092344; ENSMUSG00000070777.
DR   GeneID; 71601; -.
DR   KEGG; mmu:71601; -.
DR   UCSC; uc012fbl.1; mouse.
DR   CTD; 125931; -.
DR   MGI; MGI:1918851; Ceacam20.
DR   VEuPathDB; HostDB:ENSMUSG00000070777; -.
DR   eggNOG; ENOG502RXPD; Eukaryota.
DR   GeneTree; ENSGT00960000186634; -.
DR   HOGENOM; CLU_032483_0_0_1; -.
DR   InParanoid; Q9D2Z1; -.
DR   OMA; FKWINGS; -.
DR   OrthoDB; 998214at2759; -.
DR   PhylomeDB; Q9D2Z1; -.
DR   TreeFam; TF331199; -.
DR   BioGRID-ORCS; 71601; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Ceacam20; mouse.
DR   PRO; PR:Q9D2Z1; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9D2Z1; protein.
DR   Bgee; ENSMUSG00000070777; Expressed in animal zygote and 24 other tissues.
DR   ExpressionAtlas; Q9D2Z1; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR   GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..577
FT                   /note="Carcinoembryonic antigen-related cell adhesion
FT                   molecule 20"
FT                   /id="PRO_5007716426"
FT   TOPO_DOM        31..430
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        452..577
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          48..137
FT                   /note="Ig-like C2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          142..223
FT                   /note="Ig-like C2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          239..324
FT                   /note="Ig-like C2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          329..415
FT                   /note="Ig-like C2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   REGION          461..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..549
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         559
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:26195794"
FT   MOD_RES         570
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:26195794"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        72..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        259..307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        358..399
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   MUTAGEN         559
FT                   /note="Y->F: Abolishes tyrosine phosphorylation and
FT                   interaction with SYK; when associated with F-570."
FT                   /evidence="ECO:0000269|PubMed:26195794"
FT   MUTAGEN         570
FT                   /note="Y->F: Abolishes tyrosine phosphorylation and
FT                   interaction with SYK; when associated with F-559."
FT                   /evidence="ECO:0000269|PubMed:26195794"
FT   CONFLICT        8
FT                   /note="C -> G (in Ref. 3; AAH49361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="T -> I (in Ref. 3; AAH49361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        484
FT                   /note="P -> L (in Ref. 3; AAH49361)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   577 AA;  63444 MW;  C3470C7B60F8BB2B CRC64;
     MELAGFHCCS WTVILLSALL PTTWRPPAAA HFIHRADLLS NTQMERAPLA KLTLTVNQST
     VTEQREMAVF YCNTNADNIT IHWVSNNSLL VLNERMKLSA DNKTLTILIV QREDSGSYLC
     EVQHGFEVQR SNTASLTVNY GPDPVSIKLD SGVAAGDVVE VMEGNTVNFR VEAQSSPVPA
     YAWYLPSDFI QPPTTGTFTI DAVSREHEGM YRCLVSNPVT NLSRLGVVKV QVLEKVTAPN
     IEFPTLALVE NATSVTLTCK TSHQRVGVHW FLKGQPLRPS DRLTLSSQNR TLTIHGLQRD
     DIGPYECEVW NWGSQARSVP LKLTINYGPD QVEITQGPAS GVVSTIEAML NSSLTLYCRA
     DSIPGARYQW THEHSSKVLD GEQLSIEALR QEHQGIYSCT SSNDVTGLAR SASVLVMVVG
     LQSSSMSPGA IAGIVIGILV AIALAIGLGY FLYSTKDRWT RRRSASDTTS SNTIPPTSVM
     QSTPESRHNK PMTVYDNTPK PEGEARGKKM WSLPRDSPEQ FYEKKPPSAA PEGPRKPLPQ
     IPKQPLMPPG PGRNEESNYE KLLNSNHSLY CKITPSA
 
 
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