GENTAUR Molecular Products.

 CLM1_HUMAN              Reviewed;         290 AA.
 Q8TDQ1; B2RCL2; C9JDN3; Q3Y6P0; Q6UX24; Q7Z6A6; Q7Z7I4; Q7Z7I5;
 Q8N6D0; Q8NAF5;
 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
 18-MAY-2010, sequence version 3.
 18-JUL-2018, entry version 132.
 RecName: Full=CMRF35-like molecule 1;
          Short=CLM-1;
 AltName: Full=CD300 antigen-like family member F;
 AltName: Full=Immune receptor expressed on myeloid cells 1;
          Short=IREM-1;
 AltName: Full=Immunoglobulin superfamily member 13;
          Short=IgSF13;
 AltName: Full=NK inhibitory receptor;
 AltName: CD_antigen=CD300f;
 Flags: Precursor;
 Name=CD300LF; Synonyms=CD300F, CLM1, IGSF13, IREM1, NKIR;
 ORFNames=UNQ3105/PRO10111;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
 INTERACTION WITH PTPN6, PHOSPHORYLATION, AND VARIANTS ALA-19 AND
 ARG-218.
 PubMed=15184070; DOI=10.1016/j.bbrc.2004.05.065;
 Sui L., Li N., Liu Q., Zhang W., Wan T., Wang B., Luo K., Sun H.,
 Cao X.;
 "IgSF13, a novel human inhibitory receptor of the immunoglobulin
 superfamily, is preferentially expressed in dendritic cells and
 monocytes.";
 Biochem. Biophys. Res. Commun. 319:920-928(2004).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 6), FUNCTION, TISSUE
 SPECIFICITY, INTERACTION WITH PTPN6, SITE, MUTAGENESIS OF TYR-205;
 TYR-249 AND TYR-284, AND VARIANTS ALA-19 AND ARG-218.
 PubMed=15549731; DOI=10.1002/eji.200425433;
 Alvarez-Errico D., Aguilar H., Kitzig F., Brckalo T., Sayos J.,
 Lopez-Botet M.;
 "IREM-1 is a novel inhibitory receptor expressed by myeloid cells.";
 Eur. J. Immunol. 34:3690-3701(2004).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
 ALA-19 AND ARG-218.
 PubMed=12975309; DOI=10.1101/gr.1293003;
 Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
 Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
 Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
 Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
 Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
 Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
 Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
 Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
 Wood W.I., Godowski P.J., Gray A.M.;
 "The secreted protein discovery initiative (SPDI), a large-scale
 effort to identify novel human secreted and transmembrane proteins: a
 bioinformatics assessment.";
 Genome Res. 13:2265-2270(2003).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND
 VARIANTS ALA-19 AND ARG-218.
 TISSUE=Small intestine, and Umbilical cord blood;
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
 ALA-19.
 Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z.,
 Liang M., Tang Z., Wen S., Li H., Yang S.;
 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16625196; DOI=10.1038/nature04689;
 Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
 Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
 Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
 Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
 DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
 Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
 Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
 Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
 Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
 Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
 Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
 Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
 Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
 Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
 "DNA sequence of human chromosome 17 and analysis of rearrangement in
 the human lineage.";
 Nature 440:1045-1049(2006).
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT
 ALA-19.
 TISSUE=Lung;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [8]
 PROTEIN SEQUENCE OF 20-34.
 PubMed=15340161; DOI=10.1110/ps.04682504;
 Zhang Z., Henzel W.J.;
 "Signal peptide prediction based on analysis of experimentally
 verified cleavage sites.";
 Protein Sci. 13:2819-2824(2004).
 [9]
 FUNCTION.
 PubMed=22043923; DOI=10.1111/j.1365-2567.2011.03528.x;
 Kim E.J., Lee S.M., Suk K., Lee W.H.;
 "CD300a and CD300f differentially regulate the MyD88 and TRIF-mediated
 TLR signalling pathways through activation of SHP-1 and/or SHP-2 in
 human monocytic cell lines.";
 Immunology 135:226-235(2012).
 [10]
 FUNCTION, CERAMIDE-BINDING, AND SPHINGOMYELIN-BINDING.
 PubMed=24035150; DOI=10.1016/j.jaci.2013.08.008;
 Izawa K., Isobe M., Matsukawa T., Ito S., Maehara A., Takahashi M.,
 Yamanishi Y., Kaitani A., Oki T., Okumura K., Kitamura T., Kitaura J.;
 "Sphingomyelin and ceramide are physiological ligands for human
 LMIR3/CD300f, inhibiting FcepsilonRI-mediated mast cell activation.";
 J. Allergy Clin. Immunol. 133:270-273(2014).
 [11]
 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-140, AND DISULFIDE BONDS.
 PubMed=17275839; DOI=10.1016/j.jmb.2007.01.011;
 Marquez J.A., Galfre E., Dupeux F., Flot D., Moran O., Dimasi N.;
 "The crystal structure of the extracellular domain of the inhibitor
 receptor expressed on myeloid cells IREM-1.";
 J. Mol. Biol. 367:310-318(2007).
 -!- FUNCTION: Acts as an inhibitory receptor for myeloid cells and
     mast cells (PubMed:15549731). Positively regulates the
     phagocytosis of apoptotic cells (efferocytosis) via
     phosphatidylserine (PS) recognition; recognizes and binds PS as a
     ligand which is expressed on the surface of apoptotic cells. Plays
     an important role in the maintenance of immune homeostasis, by
     promoting macrophage-mediated efferocytosis and by inhibiting
     dendritic cell-mediated efferocytosis (By similarity). Negatively
     regulates Fc epsilon receptor-dependent mast cell activation and
     allergic responses via binding to ceramide and sphingomyelin which
     act as ligands (PubMed:24035150). May act as a coreceptor for
     interleukin 4 (IL-4). Associates with and regulates IL-4 receptor
     alpha-mediated responses by augmenting IL-4- and IL-13-induced
     signaling (By similarity). Negatively regulates the Toll-like
     receptor (TLR) signaling mediated by MYD88 and TRIF through
     activation of PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:22043923).
     Inhibits osteoclast formation. Induces macrophage cell death upon
     engagement (By similarity). {ECO:0000250|UniProtKB:Q6SJQ7,
     ECO:0000269|PubMed:15549731, ECO:0000269|PubMed:22043923,
     ECO:0000269|PubMed:24035150}.
 -!- SUBUNIT: Interacts with PTPN6/SHP-1 in a tyrosine phosphorylation
     dependent manner (PubMed:15184070, PubMed:15549731). Interacts
     with IL4R (By similarity). {ECO:0000250|UniProtKB:Q6SJQ7,
     ECO:0000269|PubMed:15184070, ECO:0000269|PubMed:15549731}.
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
     type I membrane protein {ECO:0000305}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=6;
     Name=1;
       IsoId=Q8TDQ1-1; Sequence=Displayed;
     Name=2;
       IsoId=Q8TDQ1-2; Sequence=VSP_020056, VSP_020057, VSP_020062,
                                VSP_020064;
       Note=No experimental confirmation available.;
     Name=3;
       IsoId=Q8TDQ1-3; Sequence=VSP_020056, VSP_020060, VSP_020061;
     Name=4;
       IsoId=Q8TDQ1-4; Sequence=VSP_020056, VSP_020058, VSP_020063;
       Note=No experimental confirmation available.;
     Name=5;
       IsoId=Q8TDQ1-5; Sequence=VSP_020059, VSP_020065;
       Note=No experimental confirmation available.;
     Name=6;
       IsoId=Q8TDQ1-6; Sequence=VSP_020056;
 -!- TISSUE SPECIFICITY: Highly expressed in spleen, peripheral blood
     leukocyte and monocyte, and lung. Weakly expressed in thymus,
     heart, brain, placenta, liver, skeletal muscle, kidney, pancreas,
     prostate, testis, ovary, small intestine or colon. Expressed
     selectively in monocytes and monocyte-related cells.
     {ECO:0000269|PubMed:15184070, ECO:0000269|PubMed:15549731}.
 -!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:15184070}.
 -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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 EMBL; AF251706; AAM19099.1; -; mRNA.
 EMBL; AF375480; AAP42152.1; -; mRNA.
 EMBL; AF375481; AAP42153.1; -; mRNA.
 EMBL; AY303545; AAP57942.1; -; mRNA.
 EMBL; AY358545; AAQ88909.1; -; mRNA.
 EMBL; AK092757; BAC03966.1; -; mRNA.
 EMBL; AK315165; BAG37609.1; -; mRNA.
 EMBL; DQ153249; AAZ81566.1; -; mRNA.
 EMBL; AC016888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC064805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC028199; AAH28199.1; -; mRNA.
 CCDS; CCDS11704.1; -. [Q8TDQ1-1]
 CCDS; CCDS74148.1; -. [Q8TDQ1-4]
 CCDS; CCDS74149.1; -. [Q8TDQ1-6]
 CCDS; CCDS74150.1; -. [Q8TDQ1-2]
 CCDS; CCDS74151.1; -. [Q8TDQ1-5]
 RefSeq; NP_001276011.1; NM_001289082.1. [Q8TDQ1-4]
 RefSeq; NP_001276012.1; NM_001289083.1. [Q8TDQ1-5]
 RefSeq; NP_001276013.1; NM_001289084.1.
 RefSeq; NP_001276014.1; NM_001289085.1. [Q8TDQ1-6]
 RefSeq; NP_001276015.1; NM_001289086.1. [Q8TDQ1-2]
 RefSeq; NP_001276016.1; NM_001289087.1.
 RefSeq; NP_620587.2; NM_139018.4. [Q8TDQ1-1]
 UniGene; Hs.567706; -.
 PDB; 2NMS; X-ray; 2.60 A; A=21-140.
 PDBsum; 2NMS; -.
 ProteinModelPortal; Q8TDQ1; -.
 SMR; Q8TDQ1; -.
 BioGrid; 127005; 1.
 IntAct; Q8TDQ1; 2.
 MINT; Q8TDQ1; -.
 STRING; 9606.ENSP00000327075; -.
 iPTMnet; Q8TDQ1; -.
 PhosphoSitePlus; Q8TDQ1; -.
 BioMuta; CD300LF; -.
 DMDM; 296439398; -.
 PaxDb; Q8TDQ1; -.
 PeptideAtlas; Q8TDQ1; -.
 PRIDE; Q8TDQ1; -.
 ProteomicsDB; 74321; -.
 ProteomicsDB; 74322; -. [Q8TDQ1-2]
 ProteomicsDB; 74323; -. [Q8TDQ1-3]
 ProteomicsDB; 74324; -. [Q8TDQ1-4]
 ProteomicsDB; 74325; -. [Q8TDQ1-5]
 ProteomicsDB; 74326; -. [Q8TDQ1-6]
 TopDownProteomics; Q8TDQ1-4; -. [Q8TDQ1-4]
 DNASU; 146722; -.
 Ensembl; ENST00000301573; ENSP00000301573; ENSG00000186074. [Q8TDQ1-5]
 Ensembl; ENST00000326165; ENSP00000327075; ENSG00000186074. [Q8TDQ1-1]
 Ensembl; ENST00000343125; ENSP00000343751; ENSG00000186074. [Q8TDQ1-4]
 Ensembl; ENST00000361254; ENSP00000355294; ENSG00000186074. [Q8TDQ1-2]
 Ensembl; ENST00000462044; ENSP00000464223; ENSG00000186074. [Q8TDQ1-3]
 Ensembl; ENST00000464910; ENSP00000464257; ENSG00000186074. [Q8TDQ1-6]
 Ensembl; ENST00000469092; ENSP00000463743; ENSG00000186074. [Q8TDQ1-4]
 Ensembl; ENST00000581500; ENSP00000464610; ENSG00000186074. [Q8TDQ1-2]
 GeneID; 146722; -.
 KEGG; hsa:146722; -.
 UCSC; uc002jlg.5; human. [Q8TDQ1-1]
 CTD; 146722; -.
 DisGeNET; 146722; -.
 EuPathDB; HostDB:ENSG00000186074.18; -.
 GeneCards; CD300LF; -.
 H-InvDB; HIX0021633; -.
 HGNC; HGNC:29883; CD300LF.
 MIM; 609807; gene.
 neXtProt; NX_Q8TDQ1; -.
 OpenTargets; ENSG00000186074; -.
 PharmGKB; PA142672153; -.
 eggNOG; ENOG410IZ4I; Eukaryota.
 eggNOG; ENOG410YT8T; LUCA.
 GeneTree; ENSGT00470000042273; -.
 HOVERGEN; HBG050999; -.
 InParanoid; Q8TDQ1; -.
 KO; K20395; -.
 PhylomeDB; Q8TDQ1; -.
 TreeFam; TF334441; -.
 Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
 EvolutionaryTrace; Q8TDQ1; -.
 GeneWiki; CD300LF; -.
 GenomeRNAi; 146722; -.
 PRO; PR:Q8TDQ1; -.
 Proteomes; UP000005640; Chromosome 17.
 Bgee; ENSG00000186074; -.
 ExpressionAtlas; Q8TDQ1; baseline and differential.
 Genevisible; Q8TDQ1; HS.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0005886; C:plasma membrane; TAS:Reactome.
 GO; GO:0097001; F:ceramide binding; IDA:UniProtKB.
 GO; GO:0005136; F:interleukin-4 receptor binding; ISS:UniProtKB.
 GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
 GO; GO:0035772; P:interleukin-13-mediated signaling pathway; ISS:UniProtKB.
 GO; GO:2000426; P:negative regulation of apoptotic cell clearance; ISS:UniProtKB.
 GO; GO:0033004; P:negative regulation of mast cell activation; IDA:UniProtKB.
 GO; GO:0034125; P:negative regulation of MyD88-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
 GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISS:UniProtKB.
 GO; GO:1902216; P:positive regulation of interleukin-4-mediated signaling pathway; ISS:UniProtKB.
 GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
 GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
 Gene3D; 2.60.40.10; -; 1.
 InterPro; IPR007110; Ig-like_dom.
 InterPro; IPR036179; Ig-like_dom_sf.
 InterPro; IPR013783; Ig-like_fold.
 InterPro; IPR003599; Ig_sub.
 InterPro; IPR013106; Ig_V-set.
 Pfam; PF07686; V-set; 1.
 SMART; SM00409; IG; 1.
 SUPFAM; SSF48726; SSF48726; 1.
 PROSITE; PS50835; IG_LIKE; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
 Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
 Immunoglobulin domain; Lipid-binding; Membrane; Phosphoprotein;
 Polymorphism; Receptor; Reference proteome; Signal; Transmembrane;
 Transmembrane helix.
 SIGNAL        1     19       {ECO:0000269|PubMed:15340161}.
 CHAIN        20    290       CMRF35-like molecule 1.
                              /FTId=PRO_0000247825.
 TOPO_DOM     20    156       Extracellular. {ECO:0000255}.
 TRANSMEM    157    177       Helical. {ECO:0000255}.
 TOPO_DOM    178    290       Cytoplasmic. {ECO:0000255}.
 DOMAIN       20    126       Ig-like V-type.
 SITE        205    205       Phosphatase-binding.
 CARBOHYD     88     88       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID     40    108       {ECO:0000255|PROSITE-ProRule:PRU00114,
                              ECO:0000269|PubMed:17275839}.
 DISULFID     54     62       {ECO:0000255|PROSITE-ProRule:PRU00114,
                              ECO:0000269|PubMed:17275839}.
 VAR_SEQ       1     14       MPLLTLYLLLFWLS -> MWLPQLDLMRVISAKSQ (in
                              isoform 2, isoform 3, isoform 4 and
                              isoform 6). {ECO:0000303|PubMed:15489334,
                              ECO:0000303|PubMed:15549731,
                              ECO:0000303|Ref.5}.
                              /FTId=VSP_020056.
 VAR_SEQ     128    128       A -> ASTPAPTTPTSTTFTA (in isoform 2).
                              {ECO:0000303|Ref.5}.
                              /FTId=VSP_020057.
 VAR_SEQ     149    191       RHKLLKLSVLLPLIFTILLLLLVAASLLAWRMMKYQQKAAG
                              MS -> SSRDVPRAGTAAPGGRPLLCRPDPAAGRNLPAKGY
                              HEAFLCPG (in isoform 4).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_020058.
 VAR_SEQ     150    244       HKLLKLSVLLPLIFTILLLLLVAASLLAWRMMKYQQKAAGM
                              SPEQVLQPLEGDLCYADLTLQLAGTSPQKATTKLSSAQVDQ
                              VEVEYVTMASLPK -> SEGSQAANYRPAAHQAQAPEAQCP
                              PAPHLHHIAAAFGGRLTLGLEDDEVPAESSRDVPRAGTAAP
                              GGRPLLCRPDPAAGRNLPAKGYHEAFLCPG (in
                              isoform 5).
                              {ECO:0000303|PubMed:14702039}.
                              /FTId=VSP_020059.
 VAR_SEQ     150    162       HKLLKLSVLLPLI -> YCSPWRATSAMQT (in
                              isoform 3).
                              {ECO:0000303|PubMed:15549731}.
                              /FTId=VSP_020060.
 VAR_SEQ     163    290       Missing (in isoform 3).
                              {ECO:0000303|PubMed:15549731}.
                              /FTId=VSP_020061.
 VAR_SEQ     187    221       AAGMSPEQVLQPLEGDLCYADLTLQLAGTSPQKAT -> GT
                              AAPGGRPLLCRPDPAAGRNLPAKGYHEAFLCPG (in
                              isoform 2). {ECO:0000303|Ref.5}.
                              /FTId=VSP_020062.
 VAR_SEQ     192    290       Missing (in isoform 4).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_020063.
 VAR_SEQ     222    290       Missing (in isoform 2).
                              {ECO:0000303|Ref.5}.
                              /FTId=VSP_020064.
 VAR_SEQ     245    290       Missing (in isoform 5).
                              {ECO:0000303|PubMed:14702039}.
                              /FTId=VSP_020065.
 VARIANT      19     19       V -> A (in dbSNP:rs35489971).
                              {ECO:0000269|PubMed:12975309,
                              ECO:0000269|PubMed:14702039,
                              ECO:0000269|PubMed:15184070,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:15549731,
                              ECO:0000269|Ref.5}.
                              /FTId=VAR_039128.
 VARIANT     218    218       Q -> R (in dbSNP:rs2034310).
                              {ECO:0000269|PubMed:12975309,
                              ECO:0000269|PubMed:14702039,
                              ECO:0000269|PubMed:15184070,
                              ECO:0000269|PubMed:15549731}.
                              /FTId=VAR_027152.
 MUTAGEN     205    205       Y->F: No interaction with PTPN6.
                              {ECO:0000269|PubMed:15549731}.
 MUTAGEN     249    249       Y->F: Interaction with PTPN6.
                              {ECO:0000269|PubMed:15549731}.
 MUTAGEN     284    284       Y->F: Interaction with PTPN6.
                              {ECO:0000269|PubMed:15549731}.
 CONFLICT     37     37       T -> A (in Ref. 5; AAZ81566).
                              {ECO:0000305}.
 CONFLICT     64     64       I -> V (in Ref. 5; AAZ81566).
                              {ECO:0000305}.
 CONFLICT     78     78       D -> N (in Ref. 2; AAP42153).
                              {ECO:0000305}.
 CONFLICT    135    135       T -> I (in Ref. 2; AAP42152).
                              {ECO:0000305}.
 CONFLICT    138    138       S -> F (in Ref. 1; AAM19099).
                              {ECO:0000305}.
 CONFLICT    212    212       L -> Q (in Ref. 2; AAP42152).
                              {ECO:0000305}.
 CONFLICT    268    268       H -> R (in Ref. 2; AAP57942).
                              {ECO:0000305}.
 STRAND       21     23       {ECO:0000244|PDB:2NMS}.
 STRAND       26     31       {ECO:0000244|PDB:2NMS}.
 STRAND       36     42       {ECO:0000244|PDB:2NMS}.
 STRAND       49     59       {ECO:0000244|PDB:2NMS}.
 STRAND       63     67       {ECO:0000244|PDB:2NMS}.
 STRAND       70     72       {ECO:0000244|PDB:2NMS}.
 STRAND       75     77       {ECO:0000244|PDB:2NMS}.
 STRAND       80     85       {ECO:0000244|PDB:2NMS}.
 TURN         86     89       {ECO:0000244|PDB:2NMS}.
 STRAND       90     95       {ECO:0000244|PDB:2NMS}.
 HELIX       100    102       {ECO:0000244|PDB:2NMS}.
 STRAND      104    112       {ECO:0000244|PDB:2NMS}.
 STRAND      115    126       {ECO:0000244|PDB:2NMS}.
 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

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