CLM1_HUMAN
ID CLM1_HUMAN Reviewed; 290 AA.
AC Q8TDQ1; B2RCL2; C9JDN3; Q3Y6P0; Q6UX24; Q7Z6A6; Q7Z7I4; Q7Z7I5; Q8N6D0;
AC Q8NAF5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=CMRF35-like molecule 1;
DE Short=CLM-1;
DE AltName: Full=CD300 antigen-like family member F;
DE AltName: Full=Immune receptor expressed on myeloid cells 1;
DE Short=IREM-1;
DE AltName: Full=Immunoglobulin superfamily member 13;
DE Short=IgSF13;
DE AltName: Full=NK inhibitory receptor;
DE AltName: CD_antigen=CD300f;
DE Flags: Precursor;
GN Name=CD300LF; Synonyms=CD300F, CLM1, IGSF13, IREM1, NKIR;
GN ORFNames=UNQ3105/PRO10111;
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] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION
RP WITH PTPN6, PHOSPHORYLATION, AND VARIANTS ALA-19 AND ARG-218.
RX PubMed=15184070; DOI=10.1016/j.bbrc.2004.05.065;
RA Sui L., Li N., Liu Q., Zhang W., Wan T., Wang B., Luo K., Sun H., Cao X.;
RT "IgSF13, a novel human inhibitory receptor of the immunoglobulin
RT superfamily, is preferentially expressed in dendritic cells and
RT monocytes.";
RL Biochem. Biophys. Res. Commun. 319:920-928(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 6), FUNCTION, TISSUE
RP SPECIFICITY, INTERACTION WITH PTPN6, SITE, MUTAGENESIS OF TYR-205; TYR-249
RP AND TYR-284, AND VARIANTS ALA-19 AND ARG-218.
RX PubMed=15549731; DOI=10.1002/eji.200425433;
RA Alvarez-Errico D., Aguilar H., Kitzig F., Brckalo T., Sayos J.,
RA Lopez-Botet M.;
RT "IREM-1 is a novel inhibitory receptor expressed by myeloid cells.";
RL Eur. J. Immunol. 34:3690-3701(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-19 AND
RP ARG-218.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND VARIANTS
RP ALA-19 AND ARG-218.
RC TISSUE=Small intestine, and Umbilical cord blood;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-19.
RA Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Tang Z., Wen S., Li H., Yang S.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ALA-19.
RC TISSUE=Lung;
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 [8]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP FUNCTION.
RX PubMed=22043923; DOI=10.1111/j.1365-2567.2011.03528.x;
RA Kim E.J., Lee S.M., Suk K., Lee W.H.;
RT "CD300a and CD300f differentially regulate the MyD88 and TRIF-mediated TLR
RT signalling pathways through activation of SHP-1 and/or SHP-2 in human
RT monocytic cell lines.";
RL Immunology 135:226-235(2012).
RN [10]
RP FUNCTION, CERAMIDE-BINDING, AND SPHINGOMYELIN-BINDING.
RX PubMed=24035150; DOI=10.1016/j.jaci.2013.08.008;
RA Izawa K., Isobe M., Matsukawa T., Ito S., Maehara A., Takahashi M.,
RA Yamanishi Y., Kaitani A., Oki T., Okumura K., Kitamura T., Kitaura J.;
RT "Sphingomyelin and ceramide are physiological ligands for human
RT LMIR3/CD300f, inhibiting FcepsilonRI-mediated mast cell activation.";
RL J. Allergy Clin. Immunol. 133:270-273(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-140, AND DISULFIDE BONDS.
RX PubMed=17275839; DOI=10.1016/j.jmb.2007.01.011;
RA Marquez J.A., Galfre E., Dupeux F., Flot D., Moran O., Dimasi N.;
RT "The crystal structure of the extracellular domain of the inhibitor
RT receptor expressed on myeloid cells IREM-1.";
RL J. Mol. Biol. 367:310-318(2007).
CC -!- FUNCTION: Acts as an inhibitory receptor for myeloid cells and mast
CC cells (PubMed:15549731). Positively regulates the phagocytosis of
CC apoptotic cells (efferocytosis) via phosphatidylserine (PS)
CC recognition; recognizes and binds PS as a ligand which is expressed on
CC the surface of apoptotic cells. Plays an important role in the
CC maintenance of immune homeostasis, by promoting macrophage-mediated
CC efferocytosis and by inhibiting dendritic cell-mediated efferocytosis
CC (By similarity). Negatively regulates Fc epsilon receptor-dependent
CC mast cell activation and allergic responses via binding to ceramide and
CC sphingomyelin which act as ligands (PubMed:24035150). May act as a
CC coreceptor for interleukin 4 (IL-4). Associates with and regulates IL-4
CC receptor alpha-mediated responses by augmenting IL-4- and IL-13-induced
CC signaling (By similarity). Negatively regulates the Toll-like receptor
CC (TLR) signaling mediated by MYD88 and TRIF through activation of
CC PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:22043923). Inhibits osteoclast
CC formation. Induces macrophage cell death upon engagement (By
CC similarity). {ECO:0000250|UniProtKB:Q6SJQ7,
CC ECO:0000269|PubMed:15549731, ECO:0000269|PubMed:22043923,
CC ECO:0000269|PubMed:24035150}.
CC -!- SUBUNIT: Interacts with PTPN6/SHP-1 in a tyrosine phosphorylation
CC dependent manner (PubMed:15184070, PubMed:15549731). Interacts with
CC IL4R (By similarity). {ECO:0000250|UniProtKB:Q6SJQ7,
CC ECO:0000269|PubMed:15184070, ECO:0000269|PubMed:15549731}.
CC -!- INTERACTION:
CC Q8TDQ1; A8K4G0: CD300LB; NbExp=3; IntAct=EBI-7381492, EBI-26499879;
CC Q8TDQ1; Q8TDQ1: CD300LF; NbExp=3; IntAct=EBI-7381492, EBI-7381492;
CC Q8TDQ1-4; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-17784261, EBI-12111538;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8TDQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDQ1-2; Sequence=VSP_020056, VSP_020057, VSP_020062,
CC VSP_020064;
CC Name=3;
CC IsoId=Q8TDQ1-3; Sequence=VSP_020056, VSP_020060, VSP_020061;
CC Name=4;
CC IsoId=Q8TDQ1-4; Sequence=VSP_020056, VSP_020058, VSP_020063;
CC Name=5;
CC IsoId=Q8TDQ1-5; Sequence=VSP_020059, VSP_020065;
CC Name=6;
CC IsoId=Q8TDQ1-6; Sequence=VSP_020056;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, peripheral blood
CC leukocyte and monocyte, and lung. Weakly expressed in thymus, heart,
CC brain, placenta, liver, skeletal muscle, kidney, pancreas, prostate,
CC testis, ovary, small intestine or colon. Expressed selectively in
CC monocytes and monocyte-related cells. {ECO:0000269|PubMed:15184070,
CC ECO:0000269|PubMed:15549731}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:15184070}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; AF251706; AAM19099.1; -; mRNA.
DR EMBL; AF375480; AAP42152.1; -; mRNA.
DR EMBL; AF375481; AAP42153.1; -; mRNA.
DR EMBL; AY303545; AAP57942.1; -; mRNA.
DR EMBL; AY358545; AAQ88909.1; -; mRNA.
DR EMBL; AK092757; BAC03966.1; -; mRNA.
DR EMBL; AK315165; BAG37609.1; -; mRNA.
DR EMBL; DQ153249; AAZ81566.1; -; mRNA.
DR EMBL; AC016888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC064805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028199; AAH28199.1; -; mRNA.
DR CCDS; CCDS11704.1; -. [Q8TDQ1-1]
DR CCDS; CCDS74148.1; -. [Q8TDQ1-4]
DR CCDS; CCDS74149.1; -. [Q8TDQ1-6]
DR CCDS; CCDS74150.1; -. [Q8TDQ1-2]
DR CCDS; CCDS74151.1; -. [Q8TDQ1-5]
DR RefSeq; NP_001276011.1; NM_001289082.1. [Q8TDQ1-4]
DR RefSeq; NP_001276012.1; NM_001289083.1. [Q8TDQ1-5]
DR RefSeq; NP_001276013.1; NM_001289084.1.
DR RefSeq; NP_001276014.1; NM_001289085.1. [Q8TDQ1-6]
DR RefSeq; NP_001276015.1; NM_001289086.1. [Q8TDQ1-2]
DR RefSeq; NP_001276016.1; NM_001289087.1.
DR RefSeq; NP_620587.2; NM_139018.4. [Q8TDQ1-1]
DR PDB; 2NMS; X-ray; 2.60 A; A=21-140.
DR PDBsum; 2NMS; -.
DR AlphaFoldDB; Q8TDQ1; -.
DR SMR; Q8TDQ1; -.
DR BioGRID; 127005; 5.
DR IntAct; Q8TDQ1; 7.
DR MINT; Q8TDQ1; -.
DR STRING; 9606.ENSP00000462309; -.
DR GlyGen; Q8TDQ1; 5 sites, 4 O-linked glycans (4 sites).
DR iPTMnet; Q8TDQ1; -.
DR PhosphoSitePlus; Q8TDQ1; -.
DR BioMuta; CD300LF; -.
DR DMDM; 296439398; -.
DR jPOST; Q8TDQ1; -.
DR MassIVE; Q8TDQ1; -.
DR PaxDb; Q8TDQ1; -.
DR PeptideAtlas; Q8TDQ1; -.
DR PRIDE; Q8TDQ1; -.
DR ProteomicsDB; 74321; -. [Q8TDQ1-1]
DR ProteomicsDB; 74322; -. [Q8TDQ1-2]
DR ProteomicsDB; 74323; -. [Q8TDQ1-3]
DR ProteomicsDB; 74324; -. [Q8TDQ1-4]
DR ProteomicsDB; 74325; -. [Q8TDQ1-5]
DR ProteomicsDB; 74326; -. [Q8TDQ1-6]
DR TopDownProteomics; Q8TDQ1-4; -. [Q8TDQ1-4]
DR Antibodypedia; 53166; 308 antibodies from 30 providers.
DR DNASU; 146722; -.
DR Ensembl; ENST00000301573.13; ENSP00000301573.9; ENSG00000186074.19. [Q8TDQ1-5]
DR Ensembl; ENST00000326165.11; ENSP00000327075.6; ENSG00000186074.19. [Q8TDQ1-1]
DR Ensembl; ENST00000343125.8; ENSP00000343751.4; ENSG00000186074.19. [Q8TDQ1-4]
DR Ensembl; ENST00000361254.8; ENSP00000355294.4; ENSG00000186074.19. [Q8TDQ1-2]
DR Ensembl; ENST00000462044.5; ENSP00000464223.1; ENSG00000186074.19. [Q8TDQ1-3]
DR Ensembl; ENST00000464910.5; ENSP00000464257.1; ENSG00000186074.19. [Q8TDQ1-6]
DR Ensembl; ENST00000469092.5; ENSP00000463743.1; ENSG00000186074.19. [Q8TDQ1-4]
DR Ensembl; ENST00000581500.1; ENSP00000464610.1; ENSG00000186074.19. [Q8TDQ1-2]
DR GeneID; 146722; -.
DR KEGG; hsa:146722; -.
DR MANE-Select; ENST00000326165.11; ENSP00000327075.6; NM_139018.5; NP_620587.2.
DR UCSC; uc002jlg.5; human. [Q8TDQ1-1]
DR CTD; 146722; -.
DR DisGeNET; 146722; -.
DR GeneCards; CD300LF; -.
DR HGNC; HGNC:29883; CD300LF.
DR HPA; ENSG00000186074; Tissue enhanced (bone marrow, lung, lymphoid tissue).
DR MIM; 609807; gene.
DR neXtProt; NX_Q8TDQ1; -.
DR OpenTargets; ENSG00000186074; -.
DR PharmGKB; PA142672153; -.
DR VEuPathDB; HostDB:ENSG00000186074; -.
DR eggNOG; ENOG502S7MA; Eukaryota.
DR GeneTree; ENSGT00940000154332; -.
DR HOGENOM; CLU_051023_4_0_1; -.
DR InParanoid; Q8TDQ1; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q8TDQ1; -.
DR TreeFam; TF334441; -.
DR PathwayCommons; Q8TDQ1; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q8TDQ1; -.
DR BioGRID-ORCS; 146722; 13 hits in 1064 CRISPR screens.
DR EvolutionaryTrace; Q8TDQ1; -.
DR GeneWiki; CD300LF; -.
DR GenomeRNAi; 146722; -.
DR Pharos; Q8TDQ1; Tbio.
DR PRO; PR:Q8TDQ1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8TDQ1; protein.
DR Bgee; ENSG00000186074; Expressed in monocyte and 108 other tissues.
DR ExpressionAtlas; Q8TDQ1; baseline and differential.
DR Genevisible; Q8TDQ1; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005136; F:interleukin-4 receptor binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0035772; P:interleukin-13-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:2000426; P:negative regulation of apoptotic cell clearance; ISS:UniProtKB.
DR GO; GO:0033004; P:negative regulation of mast cell activation; IDA:UniProtKB.
DR GO; GO:0034125; P:negative regulation of MyD88-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISS:UniProtKB.
DR GO; GO:1902216; P:positive regulation of interleukin-4-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Lipid-binding; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 20..290
FT /note="CMRF35-like molecule 1"
FT /id="PRO_0000247825"
FT TOPO_DOM 20..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..126
FT /note="Ig-like V-type"
FT REGION 267..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 205
FT /note="Phosphatase-binding"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17275839"
FT DISULFID 54..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17275839"
FT VAR_SEQ 1..14
FT /note="MPLLTLYLLLFWLS -> MWLPQLDLMRVISAKSQ (in isoform 2,
FT isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15549731, ECO:0000303|Ref.5"
FT /id="VSP_020056"
FT VAR_SEQ 128
FT /note="A -> ASTPAPTTPTSTTFTA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_020057"
FT VAR_SEQ 149..191
FT /note="RHKLLKLSVLLPLIFTILLLLLVAASLLAWRMMKYQQKAAGMS -> SSRDV
FT PRAGTAAPGGRPLLCRPDPAAGRNLPAKGYHEAFLCPG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020058"
FT VAR_SEQ 150..244
FT /note="HKLLKLSVLLPLIFTILLLLLVAASLLAWRMMKYQQKAAGMSPEQVLQPLEG
FT DLCYADLTLQLAGTSPQKATTKLSSAQVDQVEVEYVTMASLPK -> SEGSQAANYRPA
FT AHQAQAPEAQCPPAPHLHHIAAAFGGRLTLGLEDDEVPAESSRDVPRAGTAAPGGRPLL
FT CRPDPAAGRNLPAKGYHEAFLCPG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020059"
FT VAR_SEQ 150..162
FT /note="HKLLKLSVLLPLI -> YCSPWRATSAMQT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15549731"
FT /id="VSP_020060"
FT VAR_SEQ 163..290
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15549731"
FT /id="VSP_020061"
FT VAR_SEQ 187..221
FT /note="AAGMSPEQVLQPLEGDLCYADLTLQLAGTSPQKAT -> GTAAPGGRPLLCR
FT PDPAAGRNLPAKGYHEAFLCPG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_020062"
FT VAR_SEQ 192..290
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020063"
FT VAR_SEQ 222..290
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_020064"
FT VAR_SEQ 245..290
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020065"
FT VARIANT 19
FT /note="V -> A (in dbSNP:rs35489971)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15184070,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15549731,
FT ECO:0000269|Ref.5"
FT /id="VAR_039128"
FT VARIANT 218
FT /note="Q -> R (in dbSNP:rs2034310)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15184070,
FT ECO:0000269|PubMed:15549731"
FT /id="VAR_027152"
FT MUTAGEN 205
FT /note="Y->F: No interaction with PTPN6."
FT /evidence="ECO:0000269|PubMed:15549731"
FT MUTAGEN 249
FT /note="Y->F: Interaction with PTPN6."
FT /evidence="ECO:0000269|PubMed:15549731"
FT MUTAGEN 284
FT /note="Y->F: Interaction with PTPN6."
FT /evidence="ECO:0000269|PubMed:15549731"
FT CONFLICT 37
FT /note="T -> A (in Ref. 5; AAZ81566)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="I -> V (in Ref. 5; AAZ81566)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="D -> N (in Ref. 2; AAP42153)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> I (in Ref. 2; AAP42152)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> F (in Ref. 1; AAM19099)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="L -> Q (in Ref. 2; AAP42152)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="H -> R (in Ref. 2; AAP57942)"
FT /evidence="ECO:0000305"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:2NMS"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2NMS"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:2NMS"
FT STRAND 115..126
FT /evidence="ECO:0007829|PDB:2NMS"
SQ SEQUENCE 290 AA; 32335 MW; 27AA95664B82B945 CRC64;
MPLLTLYLLL FWLSGYSIVT QITGPTTVNG LERGSLTVQC VYRSGWETYL KWWCRGAIWR
DCKILVKTSG SEQEVKRDRV SIKDNQKNRT FTVTMEDLMK TDADTYWCGI EKTGNDLGVT
VQVTIDPAPV TQEETSSSPT LTGHHLDNRH KLLKLSVLLP LIFTILLLLL VAASLLAWRM
MKYQQKAAGM SPEQVLQPLE GDLCYADLTL QLAGTSPQKA TTKLSSAQVD QVEVEYVTMA
SLPKEDISYA SLTLGAEDQE PTYCNMGHLS SHLPGRGPEE PTEYSTISRP
