ITA2B_MOUSE
ID ITA2B_MOUSE Reviewed; 1033 AA.
AC Q9QUM0; Q3U3R7; Q64229; Q9Z2M0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Integrin alpha-IIb;
DE AltName: Full=GPalpha IIb;
DE Short=GPIIb;
DE AltName: Full=Platelet membrane glycoprotein IIb;
DE AltName: CD_antigen=CD41;
DE Contains:
DE RecName: Full=Integrin alpha-IIb heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-IIb light chain;
DE Flags: Precursor;
GN Name=Itga2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10572112;
RA Thornton M.A., Poncz M.;
RT "Characterization of the murine platelet alphaIIb gene and encoded cDNA.";
RL Blood 94:3947-3950(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 805-865.
RX PubMed=1512266; DOI=10.1016/s0021-9258(18)41927-8;
RA Chen Y.Q., Gao X., Timar J., Tang D., Grossi I.M., Chelladurai M.,
RA Kunicki T.J., Fligiel S.E., Taylor J.D., Honn K.V.;
RT "Identification of the alpha IIb beta 3 integrin in murine tumor cells.";
RL J. Biol. Chem. 267:17314-17320(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 790-1022.
RA Rout U.K., Armant D.R.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-484.
RX PubMed=10713093; DOI=10.1074/jbc.275.11.7795;
RA Puzon-McLaughlin W., Kamata T., Takada Y.;
RT "Multiple discontinuous ligand-mimetic antibody binding sites define a
RT ligand binding pocket in integrin alphaIIbbeta3.";
RL J. Biol. Chem. 275:7795-7802(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH PPIA.
RX PubMed=24429998; DOI=10.1160/th13-09-0738;
RA Wang L., Soe N.N., Sowden M., Xu Y., Modjeski K., Baskaran P., Kim Y.,
RA Smolock E.M., Morrell C.N., Berk B.C.;
RT "Cyclophilin A is an important mediator of platelet function by regulating
RT integrin alphaIIbbeta3 bidirectional signalling.";
RL Thromb. Haemost. 111:873-882(2014).
CC -!- FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin,
CC fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin.
CC It recognizes the sequence R-G-D in a wide array of ligands. It
CC recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma
CC chain. Following activation integrin alpha-IIb/beta-3 brings about
CC platelet/platelet interaction through binding of soluble fibrinogen.
CC This step leads to rapid platelet aggregation which physically plugs
CC ruptured endothelial cell surface.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond.
CC Alpha-IIb associates with beta-3. Directly interacts with RNF181.
CC Interacts (via C-terminus cytoplasmic tail region) with CIB1; the
CC interaction is direct and calcium-dependent. Interacts (via C-terminus
CC cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are
CC stabilized/increased in a calcium and magnesium-dependent manner (By
CC similarity). ITGA2B:ITGB3 interacts with PPIA/CYPA; the interaction is
CC ROS and PPIase activity-dependent and is increased in the presence of
CC thrombin (PubMed:24429998). {ECO:0000250|UniProtKB:P08514,
CC ECO:0000269|PubMed:24429998}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AF169829; AAF06996.1; -; Genomic_DNA.
DR EMBL; AF170316; AAD56216.1; -; mRNA.
DR EMBL; AK142289; BAE25013.1; -; mRNA.
DR EMBL; AK154619; BAE32718.1; -; mRNA.
DR EMBL; AL596258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120493; AAI20494.1; -; mRNA.
DR EMBL; S43388; AAB23054.2; -; mRNA.
DR EMBL; AF045019; AAD02339.1; -; mRNA.
DR EMBL; AF166384; AAF43997.1; -; mRNA.
DR CCDS; CCDS25500.1; -.
DR PIR; A43430; A43430.
DR RefSeq; NP_034705.2; NM_010575.2.
DR AlphaFoldDB; Q9QUM0; -.
DR SMR; Q9QUM0; -.
DR BioGRID; 200815; 147.
DR ComplexPortal; CPX-3116; Integrin alphaIIb-beta3 complex.
DR STRING; 10090.ENSMUSP00000099375; -.
DR BindingDB; Q9QUM0; -.
DR ChEMBL; CHEMBL3430894; -.
DR GlyGen; Q9QUM0; 5 sites.
DR iPTMnet; Q9QUM0; -.
DR PhosphoSitePlus; Q9QUM0; -.
DR SwissPalm; Q9QUM0; -.
DR jPOST; Q9QUM0; -.
DR MaxQB; Q9QUM0; -.
DR PaxDb; Q9QUM0; -.
DR PRIDE; Q9QUM0; -.
DR ProteomicsDB; 269343; -.
DR Antibodypedia; 4350; 1958 antibodies from 51 providers.
DR DNASU; 16399; -.
DR Ensembl; ENSMUST00000103086; ENSMUSP00000099375; ENSMUSG00000034664.
DR GeneID; 16399; -.
DR KEGG; mmu:16399; -.
DR UCSC; uc007lrx.2; mouse.
DR CTD; 3674; -.
DR MGI; MGI:96601; Itga2b.
DR VEuPathDB; HostDB:ENSMUSG00000034664; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000160724; -.
DR HOGENOM; CLU_004111_4_1_1; -.
DR InParanoid; Q9QUM0; -.
DR OMA; LQMDTAN; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; Q9QUM0; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR BioGRID-ORCS; 16399; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Itga2b; mouse.
DR PRO; PR:Q9QUM0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QUM0; protein.
DR Bgee; ENSMUSG00000034664; Expressed in blood and 106 other tissues.
DR Genevisible; Q9QUM0; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..1033
FT /note="Integrin alpha-IIb"
FT /id="PRO_0000016278"
FT CHAIN 32..?
FT /note="Integrin alpha-IIb heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016279"
FT CHAIN ?..1033
FT /note="Integrin alpha-IIb light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016280"
FT TOPO_DOM 32..988
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1015..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 35..96
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 109..173
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 184..237
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 252..304
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 305..370
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 372..431
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 434..495
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1017..1021
FT /note="GFFKR motif"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..96
FT /evidence="ECO:0000250"
FT DISULFID 138..161
FT /evidence="ECO:0000250"
FT DISULFID 177..197
FT /evidence="ECO:0000250"
FT DISULFID 503..514
FT /evidence="ECO:0000250"
FT DISULFID 520..575
FT /evidence="ECO:0000250"
FT DISULFID 632..638
FT /evidence="ECO:0000250"
FT DISULFID 704..717
FT /evidence="ECO:0000250"
FT DISULFID 856..905
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 911..916
FT /evidence="ECO:0000250"
FT CONFLICT 236
FT /note="S -> T (in Ref. 1; AAF06996/AAD56216)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="A -> S (in Ref. 1; AAF06996/AAD56216)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="D -> G (in Ref. 7; AAF43997)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="G -> W (in Ref. 1; AAF06996/AAD56216)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="V -> G (in Ref. 1; AAF06996/AAD56216)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="R -> S (in Ref. 1; AAF06996/AAD56216)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="P -> H (in Ref. 6; AAD02339)"
FT /evidence="ECO:0000305"
FT CONFLICT 848..849
FT /note="VQ -> LR (in Ref. 6; AAD02339)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="D -> E (in Ref. 5; AAB23054)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="V -> A (in Ref. 1; AAF06996/AAD56216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1033 AA; 112678 MW; 7B4826E32B9130B1 CRC64;
MARASCAWHS LWLLQWTPLF LGPSAVPPVW ALNLDSEKFS VYAGPNGSHF GFSVDFHKDK
HGSVSIVVGA PRALNASQEE TGAVFLCPWK ANGGKCNPLL FDLRDETRNL GFQIFQTFKT
GQGLGASVVS WNDVIVACAP WQHWNVLEKR DEAEKTPVGG CFLAQLQSGG RAEYSPCRAN
TMSSVYAESF RGDKRYCEAG FSLAVTQAGE LVLGAPGGYF FLGLLARVPI ENIISSYRPG
TLLWHVSNQR FTYDNSNPVF FDGYRGYSVA VGEFDGDPST TEYVSGAPTW SWTLGAVEIL
DSYYQPLHRL HGEQMASYFG HSVAVTDVNG DGRHDLLVGA PLYMESRADR KLAEVGRVYL
FLQPKGPQAL STPTLLLTGT QLYGRFGSAI APLGDLNRDG YNDIAVAAPY GGPSGQGQVL
IFLGQSEGLS PRPSQVLDSP FPTGSGFGFS LRGAVDIDDN GYPDLIVGAY GASKVAVYRA
QPVVMATVQL MVQDSLNPTL KNCVLDQTKT PVSCFNIQMC VGATGHNIPQ KLHLKAELQL
DLQKPRQGRR VLLLASQQAS LTLSLDLGGR DKPICHTTGA FLRDEADFRD KLSPIVLSLN
VSLPPEETGG APAVVLHGET HVQEQTRIIL DCGEDDLCVP QLRLTATAGD SPLLIGADNV
LELKIEAAND GEGAYEAELA VHLPPGAHYM RALSNIEGFE RLVCTQKKEN ESRVALCELG
NPMKKDTRIG ITMLVSVENL EEAGESVSFQ LQVRSKNSQN PNSKVVMLPV AIQAEATVEL
RGNSFPASLV VAAEEGDREQ EDLDRWVSRL EHTYELHNIG PGTVNGLRLL IHIPGQSQPS
DLLYILDVQP QGGLLCSTQP SPKVDWKLST PSPSSIRPVH HQRERRQAFL QGPKPGQQDP
VLVSCDGSAS CTVVECELRE MVRGQRAMVT VQVMLGLSSL RQRPQEQFVL QSHAWFNVSS
LPYSVPVVSL PSGQARVQTQ LLRALEERAI PVWWVLVGVL GGLLLLTLLV LAMWKAGFFK
RNRPPLEEDE EEE
