CLMP_MOUSE
ID CLMP_MOUSE Reviewed; 373 AA.
AC Q8R373; Q920S5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=CXADR-like membrane protein;
DE AltName: Full=Adipocyte adhesion molecule;
DE AltName: Full=Adipocyte-specific protein 5;
DE AltName: Full=Coxsackie- and adenovirus receptor-like membrane protein;
DE Short=CAR-like membrane protein;
DE Flags: Precursor;
GN Name=Clmp; Synonyms=Acam, Asam, Asp5;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=14573622; DOI=10.1074/jbc.m308249200;
RA Raschperger E., Engstrom U., Pettersson R.F., Fuxe J.;
RT "CLMP, a novel member of the CTX family and a new component of epithelial
RT tight junctions.";
RL J. Biol. Chem. 279:796-804(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster;
RX PubMed=15563274; DOI=10.1042/bj20041709;
RA Eguchi J., Wada J., Hida K., Zhang H., Matsuoka T., Baba M., Hashimoto I.,
RA Shikata K., Ogawa N., Makino H.;
RT "Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene
RT family, implicated in adipocyte maturation and development of obesity.";
RL Biochem. J. 387:343-353(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tsuruga H.;
RT "Adipocyte-specific protein 5, a novel protein upregulated during adipocyte
RT differentiation.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-73.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
CC -!- FUNCTION: May be involved in the cell-cell adhesion. May play a role in
CC adipocyte differentiation and development of obesity. Is required for
CC normal small intestine development (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:14573622}. Cell membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in epithelial cells within
CC different tissues and in the white adipose tissue. Expressed at high
CC levels in the heart and brain, at intermediate levels in the lung,
CC skeletal muscle, kidney and testis and at low levels in the liver and
CC spleen. {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274}.
CC -!- INDUCTION: Up-regulated in mature adipocytes and adipocyte tissue of
CC obese animals. {ECO:0000269|PubMed:15563274}.
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DR EMBL; AY259213; AAP15240.1; -; mRNA.
DR EMBL; AY326421; AAP88385.1; -; mRNA.
DR EMBL; AB040490; BAB68503.1; -; mRNA.
DR EMBL; AK033723; BAC28446.1; -; mRNA.
DR EMBL; BC026447; AAH26447.1; -; mRNA.
DR CCDS; CCDS23082.1; -.
DR RefSeq; NP_598494.2; NM_133733.4.
DR AlphaFoldDB; Q8R373; -.
DR SMR; Q8R373; -.
DR STRING; 10090.ENSMUSP00000034522; -.
DR GlyGen; Q8R373; 2 sites.
DR iPTMnet; Q8R373; -.
DR PhosphoSitePlus; Q8R373; -.
DR MaxQB; Q8R373; -.
DR PaxDb; Q8R373; -.
DR PRIDE; Q8R373; -.
DR ProteomicsDB; 279113; -.
DR Antibodypedia; 1118; 234 antibodies from 29 providers.
DR DNASU; 71566; -.
DR Ensembl; ENSMUST00000034522; ENSMUSP00000034522; ENSMUSG00000032024.
DR GeneID; 71566; -.
DR KEGG; mmu:71566; -.
DR UCSC; uc009ozt.1; mouse.
DR CTD; 79827; -.
DR MGI; MGI:1918816; Clmp.
DR VEuPathDB; HostDB:ENSMUSG00000032024; -.
DR eggNOG; KOG3866; Eukaryota.
DR GeneTree; ENSGT00940000161031; -.
DR HOGENOM; CLU_040549_0_1_1; -.
DR InParanoid; Q8R373; -.
DR OMA; RYSCKVK; -.
DR OrthoDB; 995551at2759; -.
DR PhylomeDB; Q8R373; -.
DR TreeFam; TF330875; -.
DR BioGRID-ORCS; 71566; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Clmp; mouse.
DR PRO; PR:Q8R373; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R373; protein.
DR Bgee; ENSMUSG00000032024; Expressed in undifferentiated genital tubercle and 241 other tissues.
DR Genevisible; Q8R373; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048565; P:digestive tract development; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042454; CLMP.
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 PANTHER; PTHR44783; PTHR44783; 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 1: Evidence at protein level;
KW Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..373
FT /note="CXADR-like membrane protein"
FT /id="PRO_0000293027"
FT TOPO_DOM 18..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..126
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..223
FT /note="Ig-like C2-type 2"
FT REGION 263..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 127
FT /note="V -> A (in Ref. 3; BAB68503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 41215 MW; 9C6288484AF95512 CRC64;
MSLFFLWLVS YYVGTLGTHT EIKRVAEEKV TLPCHHQLGL PEKDTLDIEW LLTDNEGNQK
VVITYSSRHV YNNLTEEQKG RVAFASNFLA GDASLQIEPL KPSDEGRYTC KVKNSGRYVW
SHVILKVLVR PSKPKCELEG EPTEGSDLTL QCESASGTKP IVYYWQRIRE KEGEDEHLPP
KSRIDYNNPG RVLLQNLTMA SSGLYQCTAG NEAGKESCVV RVTVQYVQSI GMVAGAVTGI
VAGALLIFLL IWLLIRRKSK DRYEEEDRPN EIREDAEAPR ARLVKPSSSS SGSRSSRSGS
SSTRSTGNSA SRSQRTLSSE AAPQQPGLAP QAYSLIGPEV RGSEPKKVHH TTLTKAETTL
STTPSQSKAF QTV
