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   27-MAR-2024, entry version 162.
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; 6.
DR   IntAct; Q8TDQ1; 7.
DR   MINT; Q8TDQ1; -.
DR   STRING; 9606.ENSP00000462309; -.
DR   GlyCosmos; Q8TDQ1; 5 sites, 4 glycans.
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; 9606-ENSP00000462309; -.
DR   PeptideAtlas; 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; 342 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   AGR; HGNC:29883; -.
DR   CTD; 146722; -.
DR   DisGeNET; 146722; -.
DR   GeneCards; CD300LF; -.
DR   HGNC; HGNC:29883; CD300LF.
DR   HPA; ENSG00000186074; Group enriched (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; 4204212at2759; -.
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 1142 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 109 other cell types or tissues.
DR   ExpressionAtlas; Q8TDQ1; baseline and differential.
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: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   CDD; cd05716; IgV_pIgR_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR11860:SF110; CMRF35-LIKE MOLECULE 1; 1.
DR   PANTHER; PTHR11860; POLYMERIC-IMMUNOGLOBULIN RECEPTOR; 1.
DR   Pfam; PF15330; SIT; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   Genevisible; Q8TDQ1; HS.
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
//