ITB5_HUMAN
ID ITB5_HUMAN Reviewed; 799 AA.
AC P18084; B0LPF8; B2RD70;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Integrin beta-5;
DE Flags: Precursor;
GN Name=ITGB5;
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].
RC TISSUE=Thymic epithelium;
RX PubMed=2328726; DOI=10.1002/j.1460-2075.1990.tb08275.x;
RA Ramaswamy H., Hemler M.E.;
RT "Cloning, primary structure and properties of a novel human integrin beta
RT subunit.";
RL EMBO J. 9:1561-1568(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2371275; DOI=10.1073/pnas.87.14.5354;
RA Suzuki S., Huang Z.S., Tanihara H.;
RT "Cloning of an integrin beta subunit exhibiting high homology with integrin
RT beta 3 subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5354-5358(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2211615; DOI=10.1016/s0021-9258(17)44878-2;
RA McLean J.W., Vestal D.J., Cheresh D.A., Bodary S.C.;
RT "cDNA sequence of the human integrin beta 5 subunit.";
RL J. Biol. Chem. 265:17126-17131(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-431.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
RP INTERACTION WITH MYO10.
RX PubMed=15156152; DOI=10.1038/ncb1136;
RA Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
RA Cheney R.E., Stromblad S.;
RT "Myosin-X provides a motor-based link between integrins and the
RT cytoskeleton.";
RL Nat. Cell Biol. 6:523-531(2004).
RN [8]
RP INTERACTION WITH CCN3.
RX PubMed=15611078; DOI=10.1074/jbc.m404903200;
RA Lin C.G., Chen C.C., Leu S.J., Grzeszkiewicz T.M., Lau L.F.;
RT "Integrin-dependent functions of the angiogenic inducer NOV (CCN3):
RT implication in wound healing.";
RL J. Biol. Chem. 280:8229-8237(2005).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS TYPE C
RP PENTON PROTEIN.
RX PubMed=20615244; DOI=10.1186/1743-422x-7-148;
RA Lyle C., McCormick F.;
RT "Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative
RT cells.";
RL Virol. J. 7:148-148(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for
CC fibronectin. It recognizes the sequence R-G-D in its ligand.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor
CC for adenovirus type C. {ECO:0000269|PubMed:20615244}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-5 (ITGB5)
CC associates with alpha-V (ITGAV). Interacts with MYO10
CC (PubMed:15156152). Interacts with DAB2. Integrin ITGAV:ITGB5 interacts
CC with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB5 interacts with
CC CCN3 (PubMed:15611078). {ECO:0000250|UniProtKB:O70309,
CC ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:15611078}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB5 interacts with
CC adenovirus type C penton protein. {ECO:0000269|PubMed:20615244}.
CC -!- INTERACTION:
CC P18084; Q9BY76: ANGPTL4; NbExp=3; IntAct=EBI-1223434, EBI-2968146;
CC P18084; Q92624: APPBP2; NbExp=3; IntAct=EBI-1223434, EBI-743771;
CC P18084; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1223434, EBI-3867333;
CC P18084; O95967: EFEMP2; NbExp=3; IntAct=EBI-1223434, EBI-743414;
CC P18084; Q13643: FHL3; NbExp=5; IntAct=EBI-1223434, EBI-741101;
CC P18084; Q7Z6J6: FRMD5; NbExp=3; IntAct=EBI-1223434, EBI-727282;
CC P18084; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1223434, EBI-618309;
CC P18084; P06756: ITGAV; NbExp=2; IntAct=EBI-1223434, EBI-298282;
CC P18084; Q15323: KRT31; NbExp=3; IntAct=EBI-1223434, EBI-948001;
CC P18084; O76011: KRT34; NbExp=3; IntAct=EBI-1223434, EBI-1047093;
CC P18084; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1223434, EBI-11959885;
CC P18084; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1223434, EBI-11749135;
CC P18084; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1223434, EBI-10172290;
CC P18084; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1223434, EBI-10171774;
CC P18084; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1223434, EBI-10172052;
CC P18084; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-1223434, EBI-751260;
CC P18084; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-1223434, EBI-11987425;
CC P18084; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-1223434, EBI-11522433;
CC P18084; Q9HD67: MYO10; NbExp=2; IntAct=EBI-1223434, EBI-307061;
CC P18084; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1223434, EBI-22310682;
CC P18084; Q8N720: ZNF655; NbExp=3; IntAct=EBI-1223434, EBI-625509;
CC P18084; P97479: Myo7a; Xeno; NbExp=8; IntAct=EBI-1223434, EBI-1149557;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; X53002; CAA37188.1; -; mRNA.
DR EMBL; M35011; AAA52707.1; -; mRNA.
DR EMBL; J05633; AAA59183.1; -; mRNA.
DR EMBL; AK315429; BAG37817.1; -; mRNA.
DR EMBL; EU332848; ABY87537.1; -; Genomic_DNA.
DR EMBL; BC006541; AAH06541.1; -; mRNA.
DR CCDS; CCDS3030.1; -.
DR PIR; A38308; A38308.
DR RefSeq; NP_002204.2; NM_002213.4.
DR AlphaFoldDB; P18084; -.
DR SMR; P18084; -.
DR BioGRID; 109899; 149.
DR ComplexPortal; CPX-1796; Integrin alphav-beta5 complex.
DR CORUM; P18084; -.
DR ELM; P18084; -.
DR IntAct; P18084; 56.
DR MINT; P18084; -.
DR STRING; 9606.ENSP00000296181; -.
DR BindingDB; P18084; -.
DR ChEMBL; CHEMBL2096675; -.
DR ChEMBL; CHEMBL4106150; -.
DR GuidetoPHARMACOLOGY; 2459; -.
DR GlyConnect; 1418; 6 N-Linked glycans (2 sites).
DR GlyGen; P18084; 8 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; P18084; -.
DR PhosphoSitePlus; P18084; -.
DR BioMuta; ITGB5; -.
DR DMDM; 124970; -.
DR CPTAC; CPTAC-1284; -.
DR EPD; P18084; -.
DR jPOST; P18084; -.
DR MassIVE; P18084; -.
DR MaxQB; P18084; -.
DR PaxDb; P18084; -.
DR PeptideAtlas; P18084; -.
DR PRIDE; P18084; -.
DR ProteomicsDB; 53546; -.
DR Antibodypedia; 963; 552 antibodies from 42 providers.
DR DNASU; 3693; -.
DR Ensembl; ENST00000296181.9; ENSP00000296181.4; ENSG00000082781.12.
DR GeneID; 3693; -.
DR KEGG; hsa:3693; -.
DR MANE-Select; ENST00000296181.9; ENSP00000296181.4; NM_002213.5; NP_002204.2.
DR UCSC; uc003eho.4; human.
DR CTD; 3693; -.
DR DisGeNET; 3693; -.
DR GeneCards; ITGB5; -.
DR HGNC; HGNC:6160; ITGB5.
DR HPA; ENSG00000082781; Low tissue specificity.
DR MIM; 147561; gene.
DR neXtProt; NX_P18084; -.
DR OpenTargets; ENSG00000082781; -.
DR PharmGKB; PA29959; -.
DR VEuPathDB; HostDB:ENSG00000082781; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_0_1_1; -.
DR InParanoid; P18084; -.
DR OMA; CECNPSH; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P18084; -.
DR TreeFam; TF105392; -.
DR PathwayCommons; P18084; -.
DR Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; P18084; -.
DR SIGNOR; P18084; -.
DR BioGRID-ORCS; 3693; 197 hits in 1089 CRISPR screens.
DR ChiTaRS; ITGB5; human.
DR GeneWiki; Integrin,_beta_5; -.
DR GenomeRNAi; 3693; -.
DR Pharos; P18084; Tbio.
DR PRO; PR:P18084; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P18084; protein.
DR Bgee; ENSG00000082781; Expressed in stromal cell of endometrium and 204 other tissues.
DR ExpressionAtlas; P18084; baseline and differential.
DR Genevisible; P18084; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0034684; C:integrin alphav-beta5 complex; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR027067; Integrin_beta-5.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF26; PTHR10082:SF26; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Integrin;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..799
FT /note="Integrin beta-5"
FT /id="PRO_0000016348"
FT TOPO_DOM 24..719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..76
FT /note="PSI"
FT DOMAIN 136..378
FT /note="VWFA"
FT REPEAT 465..512
FT /note="I"
FT REPEAT 513..554
FT /note="II"
FT REPEAT 555..593
FT /note="III"
FT REPEAT 594..630
FT /note="IV"
FT REGION 465..630
FT /note="Cysteine-rich tandem repeats"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..463
FT /evidence="ECO:0000250"
FT DISULFID 36..46
FT /evidence="ECO:0000250"
FT DISULFID 39..75
FT /evidence="ECO:0000250"
FT DISULFID 49..64
FT /evidence="ECO:0000250"
FT DISULFID 202..211
FT /evidence="ECO:0000250"
FT DISULFID 259..300
FT /evidence="ECO:0000250"
FT DISULFID 401..413
FT /evidence="ECO:0000250"
FT DISULFID 433..682
FT /evidence="ECO:0000250"
FT DISULFID 461..465
FT /evidence="ECO:0000250"
FT DISULFID 476..487
FT /evidence="ECO:0000250"
FT DISULFID 484..522
FT /evidence="ECO:0000250"
FT DISULFID 489..498
FT /evidence="ECO:0000250"
FT DISULFID 500..513
FT /evidence="ECO:0000250"
FT DISULFID 528..533
FT /evidence="ECO:0000250"
FT DISULFID 530..563
FT /evidence="ECO:0000250"
FT DISULFID 535..548
FT /evidence="ECO:0000250"
FT DISULFID 550..555
FT /evidence="ECO:0000250"
FT DISULFID 569..574
FT /evidence="ECO:0000250"
FT DISULFID 571..602
FT /evidence="ECO:0000250"
FT DISULFID 576..585
FT /evidence="ECO:0000250"
FT DISULFID 587..594
FT /evidence="ECO:0000250"
FT DISULFID 608..613
FT /evidence="ECO:0000250"
FT DISULFID 610..657
FT /evidence="ECO:0000250"
FT DISULFID 615..625
FT /evidence="ECO:0000250"
FT DISULFID 628..631
FT /evidence="ECO:0000250"
FT DISULFID 635..644
FT /evidence="ECO:0000250"
FT DISULFID 641..714
FT /evidence="ECO:0000250"
FT DISULFID 661..690
FT /evidence="ECO:0000250"
FT VARIANT 428
FT /note="L -> V (in dbSNP:rs2291090)"
FT /id="VAR_024290"
FT VARIANT 431
FT /note="R -> Q (in dbSNP:rs2291089)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_049634"
FT VARIANT 477
FT /note="N -> S (in dbSNP:rs2291087)"
FT /id="VAR_049635"
FT CONFLICT 193
FT /note="T -> A (in Ref. 2; AAA52707)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="L -> P (in Ref. 3; AAA59183)"
FT /evidence="ECO:0000305"
FT CONFLICT 790..792
FT /note="Missing (in Ref. 2; AAA52707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 88054 MW; D7E4727CA310512B CRC64;
MPRAPAPLYA CLLGLCALLP RLAGLNICTS GSATSCEECL LIHPKCAWCS KEDFGSPRSI
TSRCDLRANL VKNGCGGEIE SPASSFHVLR SLPLSSKGSG SAGWDVIQMT PQEIAVNLRP
GDKTTFQLQV RQVEDYPVDL YYLMDLSLSM KDDLDNIRSL GTKLAEEMRK LTSNFRLGFG
SFVDKDISPF SYTAPRYQTN PCIGYKLFPN CVPSFGFRHL LPLTDRVDSF NEEVRKQRVS
RNRDAPEGGF DAVLQAAVCK EKIGWRKDAL HLLVFTTDDV PHIALDGKLG GLVQPHDGQC
HLNEANEYTA SNQMDYPSLA LLGEKLAENN INLIFAVTKN HYMLYKNFTA LIPGTTVEIL
DGDSKNIIQL IINAYNSIRS KVELSVWDQP EDLNLFFTAT CQDGVSYPGQ RKCEGLKIGD
TASFEVSLEA RSCPSRHTEH VFALRPVGFR DSLEVGVTYN CTCGCSVGLE PNSARCNGSG
TYVCGLCECS PGYLGTRCEC QDGENQSVYQ NLCREAEGKP LCSGRGDCSC NQCSCFESEF
GKIYGPFCEC DNFSCARNKG VLCSGHGECH CGECKCHAGY IGDNCNCSTD ISTCRGRDGQ
ICSERGHCLC GQCQCTEPGA FGEMCEKCPT CPDACSTKRD CVECLLLHSG KPDNQTCHSL
CRDEVITWVD TIVKDDQEAV LCFYKTAKDC VMMFTYVELP SGKSNLTVLR EPECGNTPNA
MTILLAVVGS ILLVGLALLA IWKLLVTIHD RREFAKFQSE RSRARYEMAS NPLYRKPIST
HTVDFTFNKF NKSYNGTVD
