CLC1B_HUMAN
ID CLC1B_HUMAN Reviewed; 229 AA.
AC Q9P126; Q6UWX7; Q8NHR6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=C-type lectin domain family 1 member B;
DE AltName: Full=C-type lectin-like receptor 2;
DE Short=CLEC-2;
GN Name=CLEC1B; Synonyms=CLEC2; ORFNames=UNQ721/PRO1384;
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, VARIANTS VAL-20
RP AND ASP-64, AND FUNCTION (MICROBIAL INFECTION).
RC TISSUE=Liver;
RX PubMed=10671229;
RX DOI=10.1002/1521-4141(200002)30:2<697::aid-immu697>3.0.co;2-m;
RA Colonna M., Samaridis J., Angman L.;
RT "Molecular characterization of two novel C-type lectin-like receptors, one
RT of which is selectively expressed in human dendritic cells.";
RL Eur. J. Immunol. 30:697-704(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP VAL-20 AND ASP-64.
RC TISSUE=Liver;
RX PubMed=16940507; DOI=10.1128/jvi.00136-06;
RA Chaipan C., Soilleux E.J., Simpson P., Hofmann H., Gramberg T., Marzi A.,
RA Geier M., Stewart E.A., Eisemann J., Steinkasserer A., Suzuki-Inoue K.,
RA Fuller G.L., Pearce A.C., Watson S.P., Hoxie J.A., Baribaud F.,
RA Poehlmann S.;
RT "DC-SIGN and CLEC-2 mediate human immunodeficiency virus type 1 capture by
RT platelets.";
RL J. Virol. 80:8951-8960(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-20;
RP PRO-24 AND ASP-64.
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS VAL-20 AND
RP ASP-64.
RC TISSUE=Testis;
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 GLYCOSYLATION, PHOSPHORYLATION, TISSUE SPECIFICITY, AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=16174766; DOI=10.1182/blood-2005-05-1994;
RA Suzuki-Inoue K., Fuller G.L.J., Garcia A., Eble J.A., Poehlmann S.,
RA Inoue O., Gartner T.K., Hughan S.C., Pearce A.C., Laing G.D.,
RA Theakston R.D.G., Schweighoffer E., Zitzmann N., Morita T.,
RA Tybulewicz V.L.J., Ozaki Y., Watson S.P.;
RT "A novel Syk-dependent mechanism of platelet activation by the C-type
RT lectin receptor CLEC-2.";
RL Blood 107:542-549(2006).
RN [7]
RP FUNCTION, INTERACTION WITH PDPN, AND GLYCOSYLATION.
RX PubMed=18215137; DOI=10.1042/bj20071216;
RA Christou C.M., Pearce A.C., Watson A.A., Mistry A.R., Pollitt A.Y.,
RA Fenton-May A.E., Johnson L.A., Jackson D.G., Watson S.P., O'Callaghan C.A.;
RT "Renal cells activate the platelet receptor CLEC-2 through podoplanin.";
RL Biochem. J. 411:133-140(2008).
RN [8]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF TYR-7.
RX PubMed=18955485; DOI=10.1074/jbc.m806895200;
RA Mori J., Pearce A.C., Spalton J.C., Grygielska B., Eble J.A.,
RA Tomlinson M.G., Senis Y.A., Watson S.P.;
RT "G6b-B inhibits constitutive and agonist-induced signaling by glycoprotein
RT VI and CLEC-2.";
RL J. Biol. Chem. 283:35419-35427(2008).
RN [9]
RP INTERACTION WITH RACK1.
RX PubMed=19785988; DOI=10.1016/j.bbrc.2009.09.087;
RA Ruan Y., Guo L., Qiao Y., Hong Y., Zhou L., Sun L., Wang L., Zhu H.,
RA Wang L., Yun X., Xie J., Gu J.;
RT "RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome
RT degradation.";
RL Biochem. Biophys. Res. Commun. 390:217-222(2009).
RN [10]
RP SUBUNIT.
RX PubMed=19824697; DOI=10.1021/bi901427d;
RA Watson A.A., Christou C.M., James J.R., Fenton-May A.E., Moncayo G.E.,
RA Mistry A.R., Davis S.J., Gilbert R.J., Chakera A., O'Callaghan C.A.;
RT "The platelet receptor CLEC-2 is active as a dimer.";
RL Biochemistry 48:10988-10996(2009).
RN [11]
RP INTERACTION WITH SYK, AND PHOSPHORYLATION AT TYR-7.
RX PubMed=20154219; DOI=10.1182/blood-2009-08-237834;
RA Hughes C.E., Pollitt A.Y., Mori J., Eble J.A., Tomlinson M.G.,
RA Hartwig J.H., O'Callaghan C.A., Fuetterer K., Watson S.P.;
RT "CLEC-2 activates Syk through dimerization.";
RL Blood 115:2947-2955(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 100-221, SUBUNIT, DISULFIDE BONDS,
RP INTERACTION WITH RHODOCYTIN, AND MUTAGENESIS OF LYS-150; LYS-171; GLU-184;
RP GLU-187; ASP-188; LYS-190 AND ASN-192.
RX PubMed=17132623; DOI=10.1074/jbc.m610383200;
RA Watson A.A., Brown J., Harlos K., Eble J.A., Walter T.S., O'Callaghan C.A.;
RT "The crystal structure and mutational binding analysis of the extracellular
RT domain of the platelet-activating receptor CLEC-2.";
RL J. Biol. Chem. 282:3165-3172(2007).
CC -!- FUNCTION: C-type lectin-like receptor that functions as a platelet
CC receptor for the lymphatic endothelial marker, PDPN (PubMed:18215137).
CC After ligand activation, signals via sequential activation of SRC and
CC SYK tyrosine kinases leading to activation of PLCG2 (PubMed:18955485).
CC {ECO:0000269|PubMed:18215137, ECO:0000269|PubMed:18955485}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the platelet-
CC aggregating snake venom protein rhodocytin. Rhodocytin binding leads to
CC tyrosine phosphorylation and this promotes the binding of spleen
CC tyrosine kinase (SYK) and initiation of downstream tyrosine
CC phosphorylation events and activation of PLCG2 (PubMed:16174766,
CC PubMed:18955485). {ECO:0000269|PubMed:18955485,
CC ECO:0000305|PubMed:16174766}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment factor for Human
CC immunodeficiency virus type 1 (HIV-1) and facilitates its capture by
CC platelets (PubMed:16940507). {ECO:0000305|PubMed:16940507}.
CC -!- SUBUNIT: Homodimer. Interacts (via cytoplasmic domain) with RACK1;
CC promotes CLEC1B ubiquitination and proteasome-mediated degradation.
CC Interacts (dimer) with SYK (via SH2 domains). Interacts with PDPN; the
CC interaction is independent of CLEC1B glycosylation and activates CLEC1B
CC (PubMed:18215137). {ECO:0000269|PubMed:17132623,
CC ECO:0000269|PubMed:18215137, ECO:0000269|PubMed:19785988,
CC ECO:0000269|PubMed:19824697, ECO:0000269|PubMed:20154219}.
CC -!- INTERACTION:
CC Q9P126-1; Q86YL7: PDPN; NbExp=2; IntAct=EBI-16130833, EBI-723160;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P126-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P126-2; Sequence=VSP_023515;
CC -!- TISSUE SPECIFICITY: Expressed preferentially in the liver. Also
CC expressed in immune cells of myeloid origin and on the surface of
CC platelets. {ECO:0000269|PubMed:10671229, ECO:0000269|PubMed:16174766,
CC ECO:0000269|PubMed:16940507}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16174766,
CC ECO:0000269|PubMed:18215137}.
CC -!- PTM: Phosphorylated on tyrosine residue in response to rhodocytin
CC binding. {ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:20154219}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=CLEC-2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_240";
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DR EMBL; AF124841; AAF36777.1; -; mRNA.
DR EMBL; AY358599; AAQ88962.1; -; mRNA.
DR EMBL; AC091814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029554; AAH29554.1; -; mRNA.
DR CCDS; CCDS41751.1; -. [Q9P126-2]
DR CCDS; CCDS41752.1; -. [Q9P126-1]
DR RefSeq; NP_001092901.1; NM_001099431.1. [Q9P126-2]
DR RefSeq; NP_057593.3; NM_016509.3. [Q9P126-1]
DR RefSeq; XP_005253439.1; XM_005253382.4. [Q9P126-1]
DR RefSeq; XP_011518987.1; XM_011520685.2. [Q9P126-2]
DR RefSeq; XP_016874884.1; XM_017019395.1. [Q9P126-1]
DR PDB; 2C6U; X-ray; 1.60 A; A=100-221.
DR PDB; 3WSR; X-ray; 1.91 A; A/B=96-221.
DR PDB; 3WWK; X-ray; 2.98 A; C/F/I/L=96-221.
DR PDBsum; 2C6U; -.
DR PDBsum; 3WSR; -.
DR PDBsum; 3WWK; -.
DR AlphaFoldDB; Q9P126; -.
DR SMR; Q9P126; -.
DR BioGRID; 119420; 3.
DR DIP; DIP-61332N; -.
DR IntAct; Q9P126; 4.
DR STRING; 9606.ENSP00000298527; -.
DR GlyGen; Q9P126; 3 sites.
DR iPTMnet; Q9P126; -.
DR PhosphoSitePlus; Q9P126; -.
DR BioMuta; CLEC1B; -.
DR DMDM; 134035066; -.
DR MassIVE; Q9P126; -.
DR PaxDb; Q9P126; -.
DR PeptideAtlas; Q9P126; -.
DR PRIDE; Q9P126; -.
DR ProteomicsDB; 83635; -. [Q9P126-1]
DR ProteomicsDB; 83636; -. [Q9P126-2]
DR Antibodypedia; 23211; 357 antibodies from 33 providers.
DR DNASU; 51266; -.
DR Ensembl; ENST00000298527.11; ENSP00000298527.6; ENSG00000165682.15. [Q9P126-1]
DR Ensembl; ENST00000348658.4; ENSP00000327169.6; ENSG00000165682.15. [Q9P126-2]
DR Ensembl; ENST00000428126.6; ENSP00000406338.2; ENSG00000165682.15. [Q9P126-2]
DR GeneID; 51266; -.
DR KEGG; hsa:51266; -.
DR MANE-Select; ENST00000298527.11; ENSP00000298527.6; NM_016509.4; NP_057593.3.
DR UCSC; uc001qwu.5; human. [Q9P126-1]
DR CTD; 51266; -.
DR DisGeNET; 51266; -.
DR GeneCards; CLEC1B; -.
DR HGNC; HGNC:24356; CLEC1B.
DR HPA; ENSG00000165682; Tissue enriched (liver).
DR MIM; 606783; gene.
DR neXtProt; NX_Q9P126; -.
DR OpenTargets; ENSG00000165682; -.
DR PharmGKB; PA142672098; -.
DR VEuPathDB; HostDB:ENSG00000165682; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162140; -.
DR HOGENOM; CLU_049894_9_0_1; -.
DR InParanoid; Q9P126; -.
DR OMA; CKNKHYL; -.
DR OrthoDB; 1201127at2759; -.
DR PhylomeDB; Q9P126; -.
DR TreeFam; TF336674; -.
DR PathwayCommons; Q9P126; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q9P126; -.
DR BioGRID-ORCS; 51266; 10 hits in 1062 CRISPR screens.
DR ChiTaRS; CLEC1B; human.
DR EvolutionaryTrace; Q9P126; -.
DR GeneWiki; CLEC1B; -.
DR GenomeRNAi; 51266; -.
DR Pharos; Q9P126; Tbio.
DR PRO; PR:Q9P126; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9P126; protein.
DR Bgee; ENSG00000165682; Expressed in monocyte and 91 other tissues.
DR ExpressionAtlas; Q9P126; baseline and differential.
DR Genevisible; Q9P126; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0030220; P:platelet formation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Lectin; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..229
FT /note="C-type lectin domain family 1 member B"
FT /id="PRO_0000280043"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 109..217
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 7..10
FT /note="ITAM"
FT /evidence="ECO:0000305|PubMed:18215137"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20154219"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17132623"
FT DISULFID 130..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17132623"
FT DISULFID 195..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17132623"
FT VAR_SEQ 22..55
FT /note="VGSASSSWWRVMALILLILCVGMVVGLVALGIWS -> A (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023515"
FT VARIANT 20
FT /note="I -> V (in dbSNP:rs612593)"
FT /evidence="ECO:0000269|PubMed:10671229,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16940507"
FT /id="VAR_031047"
FT VARIANT 24
FT /note="S -> P (in dbSNP:rs2273986)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_031048"
FT VARIANT 28
FT /note="S -> F (in dbSNP:rs2273987)"
FT /id="VAR_031049"
FT VARIANT 64
FT /note="G -> D (in dbSNP:rs583903)"
FT /evidence="ECO:0000269|PubMed:10671229,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16940507"
FT /id="VAR_031050"
FT MUTAGEN 7
FT /note="Y->F: Loss of activation upon podoplanin or
FT rhodocytin stimulation."
FT /evidence="ECO:0000269|PubMed:18955485"
FT MUTAGEN 150
FT /note="K->A: Substantial reduction in rhodocytin binding."
FT /evidence="ECO:0000269|PubMed:17132623"
FT MUTAGEN 171
FT /note="K->A: Significant reduction in rhodocytin binding."
FT /evidence="ECO:0000269|PubMed:17132623"
FT MUTAGEN 184
FT /note="E->A: Significant reduction in rhodocytin binding."
FT /evidence="ECO:0000269|PubMed:17132623"
FT MUTAGEN 187
FT /note="E->A: Significant reduction in rhodocytin binding."
FT /evidence="ECO:0000269|PubMed:17132623"
FT MUTAGEN 188
FT /note="D->A: Significant reduction in rhodocytin binding."
FT /evidence="ECO:0000269|PubMed:17132623"
FT MUTAGEN 190
FT /note="K->A: Significant reduction in rhodocytin binding."
FT /evidence="ECO:0000269|PubMed:17132623"
FT MUTAGEN 192
FT /note="N->A: Significant reduction in rhodocytin binding."
FT /evidence="ECO:0000269|PubMed:17132623"
FT CONFLICT 41
FT /note="C -> Y (in Ref. 1; AAF36777 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2C6U"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:2C6U"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:2C6U"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:2C6U"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2C6U"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:2C6U"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2C6U"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2C6U"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2C6U"
SQ SEQUENCE 229 AA; 26596 MW; B39BF202AAE6DDD9 CRC64;
MQDEDGYITL NIKTRKPALI SVGSASSSWW RVMALILLIL CVGMVVGLVA LGIWSVMQRN
YLQGENENRT GTLQQLAKRF CQYVVKQSEL KGTFKGHKCS PCDTNWRYYG DSCYGFFRHN
LTWEESKQYC TDMNATLLKI DNRNIVEYIK ARTHLIRWVG LSRQKSNEVW KWEDGSVISE
NMFEFLEDGK GNMNCAYFHN GKMHPTFCEN KHYLMCERKA GMTKVDQLP
