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CMRF35-like molecule 1 (CLM-1) (CD300 antigen-like family member F) (Immune receptor expressed on myeloid cells 1) (IREM-1) (Immunoglobulin superfamily member 13) (IgSF13) (NK inhibitory receptor) (CD antigen CD300f)

 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.
28-FEB-2018, entry version 130.
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; 1.
MINT; Q8TDQ1; -.
STRING; 9606.ENSP00000327075; -.
iPTMnet; Q8TDQ1; -.
PhosphoSitePlus; Q8TDQ1; -.
BioMuta; CD300LF; -.
DMDM; 296439398; -.
PaxDb; Q8TDQ1; -.
PeptideAtlas; Q8TDQ1; -.
PRIDE; Q8TDQ1; -.
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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