CLMP_HUMAN
ID CLMP_HUMAN Reviewed; 373 AA.
AC Q9H6B4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=CXADR-like membrane protein;
DE AltName: Full=Adipocyte adhesion molecule;
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; ORFNames=UNQ318/PRO363;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [5]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP VARIANT CSBS ASP-124, AND CHARACTERIZATION OF VARIANT CSBS ASP-124.
RX PubMed=22155368; DOI=10.1053/j.gastro.2011.11.038;
RA Van Der Werf C.S., Wabbersen T.D., Hsiao N.H., Paredes J., Etchevers H.C.,
RA Kroisel P.M., Tibboel D., Babarit C., Schreiber R.A., Hoffenberg E.J.,
RA Vekemans M., Zeder S.L., Ceccherini I., Lyonnet S., Ribeiro A.S.,
RA Seruca R., Te Meerman G.J., van Ijzendoorn S.C., Shepherd I.T.,
RA Verheij J.B., Hofstra R.M.;
RT "CLMP is required for intestinal development, and loss-of-function
RT mutations cause congenital short-bowel syndrome.";
RL Gastroenterology 142:453-462(2012).
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. {ECO:0000269|PubMed:14573622,
CC ECO:0000269|PubMed:15563274, ECO:0000269|PubMed:22155368}.
CC -!- INTERACTION:
CC Q9H6B4; P80188: LCN2; NbExp=3; IntAct=EBI-4314260, EBI-11911016;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:22155368}. Cell
CC membrane {ECO:0000305}; Single-pass type I membrane protein
CC {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 small intestine and placenta, at intermediate levels in the
CC heart, skeletal muscle, colon, spleen, kidney and lung and at low
CC levels in the liver and peripheral blood leukocytes. Highly abundant in
CC the intestine during embryo and fetal development (at protein level).
CC {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274,
CC ECO:0000269|PubMed:22155368}.
CC -!- DEVELOPMENTAL STAGE: At 7 and 8 weeks of development, it is highly
CC abundant in the rapidly dividing cells of the central and peripheral
CC nervous systems, the mesenchyme of the frontonasal and mandibular
CC processes and the dermamyotome, and it is expressed in the endodermal
CC derivatives of the foregut, midgut, and hindgut, as well as in the
CC liver, lung, esophagus, and trachea. During midterm fetal stages, 18
CC and 23 weeks of development, increased expression is observed in the
CC intestinal crypts. Midterm liver and kidney tissues strongly express
CC CLMP in the parenchyma of the lobules and cortex, respectively.
CC {ECO:0000269|PubMed:22155368}.
CC -!- INDUCTION: Up-regulated in mature adipocytes and adipocyte tissue of
CC obese individuals. {ECO:0000269|PubMed:15563274}.
CC -!- DISEASE: Congenital short bowel syndrome (CSBS) [MIM:615237]: A disease
CC characterized by a shortened small intestine, intestinal malrotation,
CC and malabsorption. The mean length of the small intestine in CSBS
CC patients is approximately 50 cm, compared with a normal length at birth
CC of 190-280 cm. Patients with CSBS may develop severe malnutrition as a
CC result of the hugely reduced absorptive surface of the small intestine.
CC Infants require parenteral nutrition for survival. However, parenteral
CC nutrition itself causes life-threatening complications such as sepsis
CC and liver failure which are associated with a high rate of mortality
CC early in life. {ECO:0000269|PubMed:22155368}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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; AY326422; AAP88386.1; -; mRNA.
DR EMBL; AY358340; AAQ88706.1; -; mRNA.
DR EMBL; AK026068; BAB15347.1; -; mRNA.
DR EMBL; BC009371; AAH09371.1; -; mRNA.
DR EMBL; BK001245; DAA01139.1; -; mRNA.
DR CCDS; CCDS8441.1; -.
DR RefSeq; NP_079045.1; NM_024769.3.
DR AlphaFoldDB; Q9H6B4; -.
DR SMR; Q9H6B4; -.
DR BioGRID; 122919; 11.
DR IntAct; Q9H6B4; 7.
DR STRING; 9606.ENSP00000405577; -.
DR GlyConnect; 1161; 1 N-Linked glycan (1 site).
DR GlyGen; Q9H6B4; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9H6B4; -.
DR PhosphoSitePlus; Q9H6B4; -.
DR BioMuta; CLMP; -.
DR DMDM; 74761472; -.
DR EPD; Q9H6B4; -.
DR jPOST; Q9H6B4; -.
DR MassIVE; Q9H6B4; -.
DR MaxQB; Q9H6B4; -.
DR PaxDb; Q9H6B4; -.
DR PeptideAtlas; Q9H6B4; -.
DR PRIDE; Q9H6B4; -.
DR ProteomicsDB; 80973; -.
DR Antibodypedia; 1118; 234 antibodies from 29 providers.
DR DNASU; 79827; -.
DR Ensembl; ENST00000448775.4; ENSP00000405577.2; ENSG00000166250.12.
DR GeneID; 79827; -.
DR KEGG; hsa:79827; -.
DR MANE-Select; ENST00000448775.4; ENSP00000405577.2; NM_024769.5; NP_079045.1.
DR UCSC; uc001pyt.4; human.
DR CTD; 79827; -.
DR DisGeNET; 79827; -.
DR GeneCards; CLMP; -.
DR HGNC; HGNC:24039; CLMP.
DR HPA; ENSG00000166250; Tissue enhanced (adipose).
DR MalaCards; CLMP; -.
DR MIM; 611693; gene.
DR MIM; 615237; phenotype.
DR neXtProt; NX_Q9H6B4; -.
DR OpenTargets; ENSG00000166250; -.
DR Orphanet; 2301; Congenital short bowel syndrome.
DR VEuPathDB; HostDB:ENSG00000166250; -.
DR eggNOG; KOG3866; Eukaryota.
DR GeneTree; ENSGT00940000161031; -.
DR HOGENOM; CLU_040549_0_1_1; -.
DR InParanoid; Q9H6B4; -.
DR OMA; RYSCKVK; -.
DR OrthoDB; 995551at2759; -.
DR PhylomeDB; Q9H6B4; -.
DR TreeFam; TF330875; -.
DR PathwayCommons; Q9H6B4; -.
DR SignaLink; Q9H6B4; -.
DR BioGRID-ORCS; 79827; 9 hits in 1062 CRISPR screens.
DR ChiTaRS; CLMP; human.
DR GenomeRNAi; 79827; -.
DR Pharos; Q9H6B4; Tbio.
DR PRO; PR:Q9H6B4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H6B4; protein.
DR Bgee; ENSG00000166250; Expressed in cartilage tissue and 155 other tissues.
DR Genevisible; Q9H6B4; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
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; PF13895; Ig_2; 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; Disease variant; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Signal; Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..373
FT /note="CXADR-like membrane protein"
FT /id="PRO_0000293026"
FT TOPO_DOM 19..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..127
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..224
FT /note="Ig-like C2-type 2"
FT REGION 264..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..327
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 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 69
FT /note="R -> H (in dbSNP:rs2276348)"
FT /id="VAR_049824"
FT VARIANT 124
FT /note="V -> D (in CSBS; affects subcellular location; the
FT mutant protein is localized in the cytoplasm;
FT dbSNP:rs587776967)"
FT /evidence="ECO:0000269|PubMed:22155368"
FT /id="VAR_069713"
SQ SEQUENCE 373 AA; 41281 MW; FDA215EB3B3C4335 CRC64;
MSLLLLLLLV SYYVGTLGTH TEIKRVAEEK VTLPCHHQLG LPEKDTLDIE WLLTDNEGNQ
KVVITYSSRH VYNNLTEEQK GRVAFASNFL AGDASLQIEP LKPSDEGRYT CKVKNSGRYV
WSHVILKVLV RPSKPKCELE GELTEGSDLT LQCESSSGTE PIVYYWQRIR EKEGEDERLP
PKSRIDYNHP GRVLLQNLTM SYSGLYQCTA GNEAGKESCV VRVTVQYVQS IGMVAGAVTG
IVAGALLIFL LVWLLIRRKD KERYEEEERP NEIREDAEAP KARLVKPSSS SSGSRSSRSG
SSSTRSTANS ASRSQRTLST DAAPQPGLAT QAYSLVGPEV RGSEPKKVHH ANLTKAETTP
SMIPSQSRAF QTV
