ID BCAM_MOUSE Reviewed; 622 AA.
AC Q9R069; Q9ESS5; Q9JKB2;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 159.
DE RecName: Full=Basal cell adhesion molecule;
DE AltName: Full=B-CAM cell surface glycoprotein;
DE AltName: Full=Lutheran antigen;
DE AltName: CD_antigen=CD239;
DE Flags: Precursor;
GN Name=Bcam; Synonyms=Gplu, Lu;
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].
RX PubMed=10630290; DOI=10.1007/s002510050602;
RA Rahuel C., Colin Y., Goossens D., Gane P., El Nemer W., Cartron J.-P.,
RA Le Van Kim C.;
RT "Characterization of a mouse laminin receptor gene homologous to the human
RT blood group Lutheran gene.";
RL Immunogenetics 50:271-277(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11507772; DOI=10.1002/dvdy.1169;
RA Moulson C.L., Li C., Miner J.H.;
RT "Localization of Lutheran, a novel laminin receptor, in normal, knockout,
RT and transgenic mice suggests an interaction with laminin alpha5 in vivo.";
RL Dev. Dyn. 222:101-114(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Taira E., Okumura S., Miki N.;
RT "Mouse Lutheran antigen.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Parsons S.F., Lee G., Chasis J.A., Tanner M.J.A., Anstee D.J.;
RT "Mouse Lutheran glycoprotein.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Lee G., Willig T.-N., Parsons S.F., Anstee D.J., Mohandas N., Chasis J.A.;
RT "Mouse Lutheran glycoprotein gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 -!- FUNCTION: Laminin alpha-5 receptor. May mediate intracellular signaling
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; AF109160; AAF14226.1; -; mRNA.
DR EMBL; AF346663; AAK83237.1; -; mRNA.
DR EMBL; AB035511; BAB16053.1; -; mRNA.
DR EMBL; AF221507; AAF34657.1; -; mRNA.
DR EMBL; AF246667; AAF61742.1; -; Genomic_DNA.
DR EMBL; AK075704; BAC35900.1; -; mRNA.
DR CCDS; CCDS39803.1; -.
DR RefSeq; NP_065232.1; NM_020486.2.
DR AlphaFoldDB; Q9R069; -.
DR SMR; Q9R069; -.
DR BioGRID; 208246; 1.
DR STRING; 10090.ENSMUSP00000003061; -.
DR GlyCosmos; Q9R069; 4 sites, 5 glycans.
DR GlyGen; Q9R069; 4 sites.
DR iPTMnet; Q9R069; -.
DR PhosphoSitePlus; Q9R069; -.
DR SwissPalm; Q9R069; -.
DR jPOST; Q9R069; -.
DR MaxQB; Q9R069; -.
DR PaxDb; 10090-ENSMUSP00000003061; -.
DR ProteomicsDB; 273733; -.
DR Antibodypedia; 17750; 487 antibodies from 35 providers.
DR DNASU; 57278; -.
DR Ensembl; ENSMUST00000003061.14; ENSMUSP00000003061.8; ENSMUSG00000002980.15.
DR GeneID; 57278; -.
DR KEGG; mmu:57278; -.
DR UCSC; uc009fnf.1; mouse.
DR AGR; MGI:1929940; -.
DR CTD; 4059; -.
DR MGI; MGI:1929940; Bcam.
DR VEuPathDB; HostDB:ENSMUSG00000002980; -.
DR eggNOG; ENOG502QWC8; Eukaryota.
DR GeneTree; ENSGT00940000161038; -.
DR HOGENOM; CLU_028888_1_0_1; -.
DR InParanoid; Q9R069; -.
DR OMA; GYMTIRT; -.
DR OrthoDB; 4211322at2759; -.
DR PhylomeDB; Q9R069; -.
DR TreeFam; TF330534; -.
DR BioGRID-ORCS; 57278; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Bcam; mouse.
DR PRO; PR:Q9R069; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R069; Protein.
DR Bgee; ENSMUSG00000002980; Expressed in interventricular septum and 137 other cell types or tissues.
DR ExpressionAtlas; Q9R069; baseline and differential.
DR Genevisible; Q9R069; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0005055; F:laminin receptor activity; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR CDD; cd00096; Ig; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR013162; CD80_C2-set.
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 PANTHER; PTHR11973:SF17; BASAL CELL ADHESION MOLECULE; 1.
DR PANTHER; PTHR11973; CELL SURFACE GLYCOPROTEIN MUC18-RELATED; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..622
FT /note="Basal cell adhesion molecule"
FT /id="PRO_0000383338"
FT TOPO_DOM 26..541
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..135
FT /note="Ig-like V-type 1"
FT DOMAIN 140..250
FT /note="Ig-like V-type 2"
FT DOMAIN 267..342
FT /note="Ig-like C2-type 1"
FT DOMAIN 356..435
FT /note="Ig-like C2-type 2"
FT DOMAIN 442..532
FT /note="Ig-like C2-type 3"
FT REGION 574..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 284..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 378..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 467..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 227
FT /note="N -> D (in Ref. 5; AAF61742)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="R -> G (in Ref. 3; BAB16053 and 5; AAF61742)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="V -> A (in Ref. 5; AAF61742)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="V -> A (in Ref. 3; BAB16053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 67670 MW; 257903F08D47EB4A CRC64;
MEPPDARAGL LWLTFLLSGY SGAQAELHVS VPPRVEVMRG EQVALDCTPR EHPEHYVLEW
FLVDGTGARH RLASVEPQGS EFLGTVHSLG RVPPYEVDSR GRLVIAKVQV GDGRDYVCVV
KAGAAGTSEA TSSVRVFATP EDTEVSPNKG TLSVMDQFAQ EIATCSSNNG NPVPRITWYR
NGQRLEVPME VNQKGYITIR TVREASGLYS LTSTLYLRLH KDDRDANFHC AAHYDLPSGQ
HGRLDSHTFR LTLHYPTEHV EFWVGSPSTT EGWVREGDAV QLLCQGDGSP SPEYSFFRQQ
GTQEEQLNVN LKGNLTLERV HRNQSGIYGC RVEDYDADEE VQLVKKLKLH VAYLDPLELS
VPEELFVFLN SSSTVVNCSA RGLPTPTVRW TKDSVTLADG PMLSLQSVTF DSAGTYTCEA
STPTVPLLSR TQSFQLIVQG APELKPNEIM PKSGNSWTEG DEVMLTCSAR GFPEPKLTWS
QRGDTPAEPP FEGRGWKSSS LMVKVTSALS REGVSCEASN IHGKKGHVFH FGSVAPQTAQ
AGVAVMAVAV SVGLLLLVVA AFYCMRRKGR PGCCRRAEKG APPAREPELS HSGSERPEHT
GLLMGGPSGG GRGGSGGFGD EC
//
