TIE1_HUMAN
ID TIE1_HUMAN Reviewed; 1138 AA.
AC P35590; B5A949; B5A950;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Tyrosine-protein kinase receptor Tie-1;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=TIE1; Synonyms=TIE;
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).
RX PubMed=1312667; DOI=10.1128/mcb.12.4.1698-1707.1992;
RA Partanen J., Armstrong E., Maekelae T.P., Korhonen J., Sandberg M.,
RA Renkonen R., Knuutila S., Huebner K., Alitalo K.;
RT "A novel endothelial cell surface receptor tyrosine kinase with
RT extracellular epidermal growth factor homology domains.";
RL Mol. Cell. Biol. 12:1698-1707(1992).
RN [2]
RP SEQUENCE REVISION.
RA Partanen J.M.;
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE SPLICING.
RX PubMed=18593464; DOI=10.1186/ar2447;
RA Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
RA Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
RT "Novel splice variants derived from the receptor tyrosine kinase
RT superfamily are potential therapeutics for rheumatoid arthritis.";
RL Arthritis Res. Ther. 10:R73-R73(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PROTEIN SEQUENCE OF 22-36.
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 [7]
RP INTERACTION WITH TEK/TIE2, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15851516; DOI=10.1083/jcb.200411105;
RA Saharinen P., Kerkela K., Ekman N., Marron M., Brindle N., Lee G.M.,
RA Augustin H., Koh G.Y., Alitalo K.;
RT "Multiple angiopoietin recombinant proteins activate the Tie1 receptor
RT tyrosine kinase and promote its interaction with Tie2.";
RL J. Cell Biol. 169:239-243(2005).
RN [8]
RP INTERACTION WITH TEK/TIE2, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20227369; DOI=10.1016/j.molcel.2010.02.007;
RA Seegar T.C., Eller B., Tzvetkova-Robev D., Kolev M.V., Henderson S.C.,
RA Nikolov D.B., Barton W.A.;
RT "Tie1-Tie2 interactions mediate functional differences between angiopoietin
RT ligands.";
RL Mol. Cell 37:643-655(2010).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-448; VAL-1104 AND HIS-1109.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [10]
RP VARIANTS LMPHM11 CYS-481; LYS-1061 AND HIS-1109, AND INVOLVEMENT IN
RP LMPHM11.
RX PubMed=32947856; DOI=10.3390/ijms21186780;
RA Michelini S., Ricci M., Veselenyiova D., Kenanoglu S., Kurti D.,
RA Baglivo M., Fiorentino A., Basha S.H., Priya S., Serrani R., Krajcovic J.,
RA Dundar M., Dautaj A., Bertelli M.;
RT "TIE1 as a Candidate Gene for Lymphatic Malformations with or without
RT Lymphedema.";
RL Int. J. Mol. Sci. 21:0-0(2020).
CC -!- FUNCTION: Transmembrane tyrosine-protein kinase that may modulate
CC TEK/TIE2 activity and contribute to the regulation of angiogenesis.
CC {ECO:0000269|PubMed:20227369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterodimer with TEK/TIE2.
CC -!- INTERACTION:
CC P35590; Q6A162: KRT40; NbExp=3; IntAct=EBI-2256865, EBI-10171697;
CC P35590; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2256865, EBI-10171774;
CC P35590; Q15238: PSG5; NbExp=3; IntAct=EBI-2256865, EBI-4314891;
CC P35590; Q93062: RBPMS; NbExp=3; IntAct=EBI-2256865, EBI-740322;
CC P35590; Q15654: TRIP6; NbExp=3; IntAct=EBI-2256865, EBI-742327;
CC P35590; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2256865, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15851516,
CC ECO:0000269|PubMed:20227369}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:20227369}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P35590-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35590-2; Sequence=VSP_047609, VSP_047610;
CC Name=3;
CC IsoId=P35590-3; Sequence=VSP_047607, VSP_047608;
CC -!- TISSUE SPECIFICITY: Specifically expressed in developing vascular
CC endothelial cells.
CC -!- PTM: Phosphorylated on tyrosine residues in response to ANGPT1, most
CC likely by TEK/TIE2. {ECO:0000269|PubMed:15851516}.
CC -!- DISEASE: Lymphatic malformation 11 (LMPHM11) [MIM:619401]: A form of
CC primary lymphedema, a disease characterized by swelling of body parts
CC due to developmental anomalies and functional defects of the lymphatic
CC system. Patients with lymphedema may suffer from recurrent local
CC infections. LMPHM11 is an autosomal dominant form characterized by
CC onset of lower extremity edema in the second or third decade of life.
CC Some affected individuals may have subclinical lymphatic malformations.
CC {ECO:0000269|PubMed:32947856}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Tie subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TIE1ID42560ch1p34.html";
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DR EMBL; X60957; CAA43290.1; -; mRNA.
DR EMBL; EU826587; ACF47623.1; -; mRNA.
DR EMBL; EU826588; ACF47624.1; -; mRNA.
DR EMBL; AC093420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038239; AAH38239.1; -; mRNA.
DR CCDS; CCDS482.1; -. [P35590-1]
DR RefSeq; NP_005415.1; NM_005424.4. [P35590-1]
DR PDB; 5N06; X-ray; 2.50 A; A/B=642-738.
DR PDBsum; 5N06; -.
DR AlphaFoldDB; P35590; -.
DR SMR; P35590; -.
DR BioGRID; 112931; 15.
DR IntAct; P35590; 31.
DR MINT; P35590; -.
DR STRING; 9606.ENSP00000361554; -.
DR BindingDB; P35590; -.
DR ChEMBL; CHEMBL5274; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P35590; -.
DR GuidetoPHARMACOLOGY; 1841; -.
DR GlyGen; P35590; 5 sites.
DR iPTMnet; P35590; -.
DR PhosphoSitePlus; P35590; -.
DR BioMuta; TIE1; -.
DR DMDM; 549081; -.
DR MassIVE; P35590; -.
DR PaxDb; P35590; -.
DR PeptideAtlas; P35590; -.
DR PRIDE; P35590; -.
DR ProteomicsDB; 55098; -. [P35590-1]
DR ProteomicsDB; 5928; -.
DR ProteomicsDB; 5929; -.
DR Antibodypedia; 32289; 729 antibodies from 39 providers.
DR DNASU; 7075; -.
DR Ensembl; ENST00000372476.8; ENSP00000361554.3; ENSG00000066056.14. [P35590-1]
DR Ensembl; ENST00000538015.1; ENSP00000440063.1; ENSG00000066056.14. [P35590-2]
DR GeneID; 7075; -.
DR KEGG; hsa:7075; -.
DR MANE-Select; ENST00000372476.8; ENSP00000361554.3; NM_005424.5; NP_005415.1.
DR UCSC; uc001ciu.4; human. [P35590-1]
DR CTD; 7075; -.
DR DisGeNET; 7075; -.
DR GeneCards; TIE1; -.
DR HGNC; HGNC:11809; TIE1.
DR HPA; ENSG00000066056; Low tissue specificity.
DR MIM; 600222; gene.
DR MIM; 619401; phenotype.
DR neXtProt; NX_P35590; -.
DR OpenTargets; ENSG00000066056; -.
DR PharmGKB; PA36516; -.
DR VEuPathDB; HostDB:ENSG00000066056; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000157693; -.
DR HOGENOM; CLU_008888_0_0_1; -.
DR InParanoid; P35590; -.
DR OMA; AKVWWRL; -.
DR OrthoDB; 707342at2759; -.
DR PhylomeDB; P35590; -.
DR TreeFam; TF317568; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P35590; -.
DR SignaLink; P35590; -.
DR SIGNOR; P35590; -.
DR BioGRID-ORCS; 7075; 19 hits in 1104 CRISPR screens.
DR ChiTaRS; TIE1; human.
DR GenomeRNAi; 7075; -.
DR Pharos; P35590; Tchem.
DR PRO; PR:P35590; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P35590; protein.
DR Bgee; ENSG00000066056; Expressed in omental fat pad and 146 other tissues.
DR Genevisible; P35590; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060854; P:branching involved in lymph vessel morphogenesis; ISS:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0045026; P:plasma membrane fusion; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; ISS:BHF-UCL.
DR GO; GO:1901201; P:regulation of extracellular matrix assembly; ISS:BHF-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0048771; P:tissue remodeling; ISS:BHF-UCL.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; ATP-binding;
KW Cell membrane; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 22..1138
FT /note="Tyrosine-protein kinase receptor Tie-1"
FT /id="PRO_0000024471"
FT TOPO_DOM 22..759
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..784
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 785..1138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 214..256
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 258..303
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 305..345
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 372..426
FT /note="Ig-like C2-type 2"
FT DOMAIN 446..545
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 548..642
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 646..739
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 839..1118
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 979
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 845..853
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1007
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 231..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 246..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 321..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 335..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 305..317
FT /note="ACAPGHFGADCRL -> VHQGHCGAREDHS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_047607"
FT VAR_SEQ 318..1138
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_047608"
FT VAR_SEQ 348..379
FT /note="DRIPQILNMASELEFNLETMPRINCAAAGNPF -> GWRDWVDTSTEKQNTD
FT EGRFGGHVSAPVGAPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_047609"
FT VAR_SEQ 380..1138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_047610"
FT VARIANT 448
FT /note="V -> M (in dbSNP:rs56302794)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041852"
FT VARIANT 481
FT /note="R -> C (in LMPHM11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32947856"
FT /id="VAR_085888"
FT VARIANT 1061
FT /note="E -> K (in LMPHM11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32947856"
FT /id="VAR_085889"
FT VARIANT 1104
FT /note="A -> V (in dbSNP:rs35573981)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041853"
FT VARIANT 1109
FT /note="R -> H (in LMPHM11; unknown pathological
FT significance; dbSNP:rs34993202)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:32947856"
FT /id="VAR_041854"
FT STRAND 648..656
FT /evidence="ECO:0007829|PDB:5N06"
FT STRAND 659..665
FT /evidence="ECO:0007829|PDB:5N06"
FT STRAND 676..682
FT /evidence="ECO:0007829|PDB:5N06"
FT STRAND 691..695
FT /evidence="ECO:0007829|PDB:5N06"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:5N06"
FT STRAND 714..728
FT /evidence="ECO:0007829|PDB:5N06"
SQ SEQUENCE 1138 AA; 125090 MW; 3B42BE33678C58A1 CRC64;
MVWRVPPFLL PILFLASHVG AAVDLTLLAN LRLTDPQRFF LTCVSGEAGA GRGSDAWGPP
LLLEKDDRIV RTPPGPPLRL ARNGSHQVTL RGFSKPSDLV GVFSCVGGAG ARRTRVIYVH
NSPGAHLLPD KVTHTVNKGD TAVLSARVHK EKQTDVIWKS NGSYFYTLDW HEAQDGRFLL
QLPNVQPPSS GIYSATYLEA SPLGSAFFRL IVRGCGAGRW GPGCTKECPG CLHGGVCHDH
DGECVCPPGF TGTRCEQACR EGRFGQSCQE QCPGISGCRG LTFCLPDPYG CSCGSGWRGS
QCQEACAPGH FGADCRLQCQ CQNGGTCDRF SGCVCPSGWH GVHCEKSDRI PQILNMASEL
EFNLETMPRI NCAAAGNPFP VRGSIELRKP DGTVLLSTKA IVEPEKTTAE FEVPRLVLAD
SGFWECRVST SGGQDSRRFK VNVKVPPVPL AAPRLLTKQS RQLVVSPLVS FSGDGPISTV
RLHYRPQDST MDWSTIVVDP SENVTLMNLR PKTGYSVRVQ LSRPGEGGEG AWGPPTLMTT
DCPEPLLQPW LEGWHVEGTD RLRVSWSLPL VPGPLVGDGF LLRLWDGTRG QERRENVSSP
QARTALLTGL TPGTHYQLDV QLYHCTLLGP ASPPAHVLLP PSGPPAPRHL HAQALSDSEI
QLTWKHPEAL PGPISKYVVE VQVAGGAGDP LWIDVDRPEE TSTIIRGLNA STRYLFRMRA
SIQGLGDWSN TVEESTLGNG LQAEGPVQES RAAEEGLDQQ LILAVVGSVS ATCLTILAAL
LTLVCIRRSC LHRRRTFTYQ SGSGEETILQ FSSGTLTLTR RPKLQPEPLS YPVLEWEDIT
FEDLIGEGNF GQVIRAMIKK DGLKMNAAIK MLKEYASEND HRDFAGELEV LCKLGHHPNI
INLLGACKNR GYLYIAIEYA PYGNLLDFLR KSRVLETDPA FAREHGTAST LSSRQLLRFA
SDAANGMQYL SEKQFIHRDL AARNVLVGEN LASKIADFGL SRGEEVYVKK TMGRLPVRWM
AIESLNYSVY TTKSDVWSFG VLLWEIVSLG GTPYCGMTCA ELYEKLPQGY RMEQPRNCDD
EVYELMRQCW RDRPYERPPF AQIALQLGRM LEARKAYVNM SLFENFTYAG IDATAEEA
