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CEAM5_MOUSE
ID   CEAM5_MOUSE             Reviewed;         947 AA.
AC   Q3UKK2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 5;
DE   AltName: Full=Pregnancy-specific glycoprotein 30;
DE   Flags: Precursor;
GN   Name=Ceacam5; Synonyms=Psg30;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
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]
RP   GENE FAMILY.
RX   PubMed=15647114; DOI=10.1186/1471-2164-6-4;
RA   McLellan A.S., Fischer B., Dveksler G., Hori T., Wynne F., Ball M.,
RA   Okumura K., Moore T., Zimmermann W.;
RT   "Structure and evolution of the mouse pregnancy-specific glycoprotein (Psg)
RT   gene locus.";
RL   BMC Genomics 6:4-4(2005).
CC   -!- FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion,
CC       intracellular signaling and tumor progression. Mediates homophilic and
CC       heterophilic cell adhesion with other carcinoembryonic antigen-related
CC       cell adhesion molecules, such as CEACAM6. Plays a role as an oncogene
CC       by promoting tumor progression; induces resistance to anoikis of
CC       colorectal carcinoma cells. {ECO:0000250|UniProtKB:P06731}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06731}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P06731};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P06731}. Apical cell
CC       membrane {ECO:0000250|UniProtKB:P06731}. Cell surface
CC       {ECO:0000250|UniProtKB:P06731}. Note=Localized to the apical glycocalyx
CC       surface. {ECO:0000250|UniProtKB:P06731}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC       {ECO:0000305}.
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DR   EMBL; AK145976; BAE26799.1; -; mRNA.
DR   CCDS; CCDS20863.1; -.
DR   RefSeq; NP_082756.1; NM_028480.2.
DR   AlphaFoldDB; Q3UKK2; -.
DR   STRING; 10090.ENSMUSP00000080582; -.
DR   GlyGen; Q3UKK2; 13 sites.
DR   PhosphoSitePlus; Q3UKK2; -.
DR   PaxDb; Q3UKK2; -.
DR   PeptideAtlas; Q3UKK2; -.
DR   PRIDE; Q3UKK2; -.
DR   DNASU; 73250; -.
DR   Ensembl; ENSMUST00000081907; ENSMUSP00000080582; ENSMUSG00000008789.
DR   GeneID; 73250; -.
DR   KEGG; mmu:73250; -.
DR   UCSC; uc009fiz.1; mouse.
DR   CTD; 1048; -.
DR   MGI; MGI:1920500; Ceacam5.
DR   VEuPathDB; HostDB:ENSMUSG00000008789; -.
DR   eggNOG; ENOG502RXPD; Eukaryota.
DR   GeneTree; ENSGT00960000186634; -.
DR   HOGENOM; CLU_310551_0_0_1; -.
DR   InParanoid; Q3UKK2; -.
DR   OrthoDB; 998214at2759; -.
DR   PhylomeDB; Q3UKK2; -.
DR   TreeFam; TF336859; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 73250; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Ceacam5; mouse.
DR   PRO; PR:Q3UKK2; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q3UKK2; protein.
DR   Bgee; ENSMUSG00000008789; Expressed in placenta and 3 other tissues.
DR   GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 8.
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; IPR013151; Immunoglobulin.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF07686; V-set; 6.
DR   SMART; SM00409; IG; 8.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 8.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane; Oncogene;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..947
FT                   /note="Carcinoembryonic antigen-related cell adhesion
FT                   molecule 5"
FT                   /id="PRO_0000378506"
FT   DOMAIN          35..132
FT                   /note="Ig-like V-type 1"
FT                   /evidence="ECO:0000250|UniProtKB:P31997,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          166..259
FT                   /note="Ig-like V-type 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          270..378
FT                   /note="Ig-like V-type 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          392..498
FT                   /note="Ig-like V-type 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          509..615
FT                   /note="Ig-like V-type 5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          642..733
FT                   /note="Ig-like V-type 6"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          746..851
FT                   /note="Ig-like V-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          859..943
FT                   /note="Ig-like C2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        578
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        698
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        709
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        816
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        823
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        878..926
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   947 AA;  106270 MW;  3FE79EE7FC560029 CRC64;
     MEASSVLPCK WCTHLQGLLL TASFLTCCHL PTTAQITIEL EPPQVIEGEN VLIRVNNLTE
     NLITLAWFRG MRIKSPQIGQ YTPATKVTVL GPGHSGRETL YSNGSLQIYN VTQEDIGFYS
     LRIINKHAEI VSITSIYLNV YSSLWTCEHP SPHAKLTIES VPPGISEGGS VLLLVKNLPQ
     NLLSLFWYKG VIAVKKFEIA RHIKATNSSV PGPAHTGRET VFSNGSLLLQ EVMQSDTGFY
     TLRTMSTDLK DEVAHVQLYM DTYLLTCYHP LQVKIESLPQ NVAVGKTVLL LVHNLPEDFQ
     AFFWYKSAYR RDTYKIAEYK RAMDATILGS AYSSREFIYN NGSMLIIDVT EDDAGYFLLE
     ILREDLKIEK AYIQLHVNSF VSNSKDSAST ARLSIESVPP SIVEGGSVLL LVHNLPKNLQ
     SLFWYKGMIA EKKSELIQHI IATSSSLPGP AHSGRETVYN NGSLLLQRVM QNDTQFYTLQ
     TMDTDLKYEV AHVQLQLDTS LSTWYHPLQV KIESLPRNVA VGKSVLFLVH NFPEVFRAFS
     WYKPAYKSHT SKIVEYHRFT DSATVGAAYR GIEVIFTNGS MVMIDVTEDD AGFYMLEILR
     EDFKVEKAYV QLHVNSFVPN SKVSVSTARL SIESVPPSIV GGESVLLLVH NLPKNLQSLF
     WYKGVIAEEK SELIQHIIAT SSSLPGPAHS GRETVYSNGS LLLQRVMQND TGFYTLLTMS
     TDLKDEIAHV QLQLDTSTCC SLLTSDQLII VPVPRNIAVG KSVLLLVCNV PKDVQTIFWY
     KSVYRTDIFK IAEYSRSMES TIWGLAHSGK EMVYTNGSLL IQNVTEHDAG LYMLEILHKD
     YKLERAHVQV HVNNPVSWPF VRVTDTTVRV QSSVVFTCFS ADPGVSIRWL FNKQSLQLTE
     RMTLSPSKCQ LSIDPVWRED AGKYQCEVSN PVSSKSSLPV RLAVIEE
 
 
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