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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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