ITA11_HUMAN
ID ITA11_HUMAN Reviewed; 1188 AA.
AC Q9UKX5; J3KQM2; Q8WYI8; Q9UKQ1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Integrin alpha-11;
DE Flags: Precursor;
GN Name=ITGA11; ORFNames=MSTP018;
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 2), AND VARIANTS ARG-524; LEU-972 AND
RP ILE-1003.
RC TISSUE=Fetal heart, and Osteoblast;
RX PubMed=10486209; DOI=10.1006/geno.1999.5909;
RA Lehnert K., Ni J., Leung E., Gough S.M., Weaver A., Yao W.P., Liu D.,
RA Wang S.-X., Morris C.M., Krissansen G.W.;
RT "Cloning, sequence analysis, and chromosomal localization of the novel
RT human integrin alpha11 subunit (ITGA11).";
RL Genomics 60:179-187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP ARG-524 AND LEU-972.
RC TISSUE=Fetal muscle, and Uterus;
RX PubMed=10464311; DOI=10.1074/jbc.274.36.25735;
RA Velling T., Kusche-Gullberg M., Sejersen T., Gullberg D.;
RT "cDNA cloning and chromosomal localization of human alpha(11) integrin. A
RT collagen-binding, I domain-containing, beta(1)-associated integrin alpha-
RT chain present in muscle tissues.";
RL J. Biol. Chem. 274:25735-25742(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-1188 (ISOFORM 1), AND
RP VARIANTS ARG-524 AND LEU-972.
RC TISSUE=Aorta;
RA Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L.,
RA Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H.,
RA Jiang Y.X., Zhao X.W., Liu S., Liu L.S., Ding J.F., Gao R.L., Qiang B.Q.,
RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 954-1188 (ISOFORM 1).
RC TISSUE=Fibroblast;
RG The European IMAGE consortium;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH RAB21, AND MUTAGENESIS OF ARG-1170.
RX PubMed=16754960; DOI=10.1083/jcb.200509019;
RA Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
RA Ivaska J.;
RT "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic
RT of beta1-integrins.";
RL J. Cell Biol. 173:767-780(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: Integrin alpha-11/beta-1 is a receptor for collagen.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-11
CC associates with beta-1. Interacts with RAB21.
CC {ECO:0000269|PubMed:16754960}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKX5-2; Sequence=VSP_053416;
CC -!- TISSUE SPECIFICITY: According to PubMed:10464311, highest levels of
CC expression in uterus and heart, intermediate levels in skeletal muscle
CC and intermediate to low levels in pancreas, kidney and placenta.
CC According to PubMed:10486209, also found in brain, colon, lung, small
CC intestine, stomach, testis, salivary glands, thyroid glands and
CC prostate. Very low levels in peripheral blood lymphocytes, fetal brain
CC and fetal liver. {ECO:0000269|PubMed:10464311}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated in differentiating fetal
CC muscle cells (in vitro).
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39001.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ITGA11ID41001ch15q23.html";
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DR EMBL; AF109681; AAF01258.1; -; mRNA.
DR EMBL; AF137378; AAD51919.2; -; mRNA.
DR EMBL; AC021553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF111799; AAL39001.1; ALT_INIT; mRNA.
DR EMBL; AL359064; CAB94392.1; -; mRNA.
DR CCDS; CCDS45291.1; -. [Q9UKX5-1]
DR RefSeq; NP_001004439.1; NM_001004439.1. [Q9UKX5-1]
DR AlphaFoldDB; Q9UKX5; -.
DR SMR; Q9UKX5; -.
DR BioGRID; 116481; 5.
DR ComplexPortal; CPX-1818; Integrin alpha11-beta1 complex.
DR CORUM; Q9UKX5; -.
DR IntAct; Q9UKX5; 3.
DR STRING; 9606.ENSP00000327290; -.
DR ChEMBL; CHEMBL5883; -.
DR TCDB; 8.A.54.1.7; the integrin (integrin) family.
DR GlyGen; Q9UKX5; 16 sites.
DR iPTMnet; Q9UKX5; -.
DR PhosphoSitePlus; Q9UKX5; -.
DR BioMuta; ITGA11; -.
DR DMDM; 313104119; -.
DR EPD; Q9UKX5; -.
DR jPOST; Q9UKX5; -.
DR MassIVE; Q9UKX5; -.
DR MaxQB; Q9UKX5; -.
DR PaxDb; Q9UKX5; -.
DR PeptideAtlas; Q9UKX5; -.
DR PRIDE; Q9UKX5; -.
DR ProteomicsDB; 84905; -. [Q9UKX5-1]
DR ABCD; Q9UKX5; 1 sequenced antibody.
DR Antibodypedia; 26308; 121 antibodies from 29 providers.
DR CPTC; Q9UKX5; 1 antibody.
DR DNASU; 22801; -.
DR Ensembl; ENST00000315757.9; ENSP00000327290.7; ENSG00000137809.17. [Q9UKX5-1]
DR Ensembl; ENST00000423218.6; ENSP00000403392.2; ENSG00000137809.17. [Q9UKX5-2]
DR GeneID; 22801; -.
DR KEGG; hsa:22801; -.
DR MANE-Select; ENST00000315757.9; ENSP00000327290.7; NM_001004439.2; NP_001004439.1.
DR UCSC; uc002ari.4; human. [Q9UKX5-1]
DR CTD; 22801; -.
DR DisGeNET; 22801; -.
DR GeneCards; ITGA11; -.
DR HGNC; HGNC:6136; ITGA11.
DR HPA; ENSG00000137809; Tissue enhanced (cervix, endometrium, smooth muscle).
DR MIM; 604789; gene.
DR neXtProt; NX_Q9UKX5; -.
DR OpenTargets; ENSG00000137809; -.
DR PharmGKB; PA29937; -.
DR VEuPathDB; HostDB:ENSG00000137809; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000155465; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; Q9UKX5; -.
DR OMA; DCKRNGR; -.
DR PhylomeDB; Q9UKX5; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; Q9UKX5; -.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR SignaLink; Q9UKX5; -.
DR SIGNOR; Q9UKX5; -.
DR BioGRID-ORCS; 22801; 10 hits in 1060 CRISPR screens.
DR ChiTaRS; ITGA11; human.
DR GenomeRNAi; 22801; -.
DR Pharos; Q9UKX5; Tbio.
DR PRO; PR:Q9UKX5; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UKX5; protein.
DR Bgee; ENSG00000137809; Expressed in descending thoracic aorta and 146 other tissues.
DR Genevisible; Q9UKX5; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0034681; C:integrin alpha11-beta1 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005518; F:collagen binding; IMP:UniProtKB.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0038064; F:collagen receptor activity; IMP:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0038065; P:collagen-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0006929; P:substrate-dependent cell migration; IMP:UniProtKB.
DR Gene3D; 2.130.10.130; -; 2.
DR Gene3D; 3.40.50.410; -; 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; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Disulfide bond; Glycoprotein;
KW Integrin; Magnesium; Membrane; Metal-binding; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1188
FT /note="Integrin alpha-11"
FT /id="PRO_0000016318"
FT TOPO_DOM 23..1141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 24..85
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 91..151
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 164..345
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 355..406
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 411..461
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 462..527
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 528..586
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 590..650
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT BINDING 488
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 551
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 553
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 555
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 613
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 615
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 617
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1059
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..83
FT /evidence="ECO:0000250"
FT DISULFID 121..139
FT /evidence="ECO:0000255"
FT DISULFID 129..159
FT /evidence="ECO:0000255"
FT DISULFID 659..668
FT /evidence="ECO:0000250"
FT DISULFID 674..729
FT /evidence="ECO:0000250"
FT DISULFID 781..787
FT /evidence="ECO:0000250"
FT DISULFID 881..893
FT /evidence="ECO:0000250"
FT VAR_SEQ 1029
FT /note="E -> EV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10486209"
FT /id="VSP_053416"
FT VARIANT 433
FT /note="V -> M (in dbSNP:rs2306022)"
FT /id="VAR_009889"
FT VARIANT 471
FT /note="M -> L (in dbSNP:rs2306024)"
FT /id="VAR_020038"
FT VARIANT 524
FT /note="L -> R (in dbSNP:rs7168069)"
FT /evidence="ECO:0000269|PubMed:10464311,
FT ECO:0000269|PubMed:10486209, ECO:0000269|Ref.4"
FT /id="VAR_009890"
FT VARIANT 891
FT /note="Q -> K (in dbSNP:rs2271725)"
FT /id="VAR_020039"
FT VARIANT 972
FT /note="P -> L (in dbSNP:rs4777035)"
FT /evidence="ECO:0000269|PubMed:10464311,
FT ECO:0000269|PubMed:10486209, ECO:0000269|Ref.4"
FT /id="VAR_009891"
FT VARIANT 1003
FT /note="M -> I"
FT /evidence="ECO:0000269|PubMed:10486209"
FT /id="VAR_009892"
FT VARIANT 1093
FT /note="L -> V"
FT /id="VAR_009894"
FT MUTAGEN 1170
FT /note="R->A: No effect on RAB21-binding."
FT /evidence="ECO:0000269|PubMed:16754960"
SQ SEQUENCE 1188 AA; 133470 MW; BFD95E57ED5D5849 CRC64;
MDLPRGLVVA WALSLWPGFT DTFNMDTRKP RVIPGSRTAF FGYTVQQHDI SGNKWLVVGA
PLETNGYQKT GDVYKCPVIH GNCTKLNLGR VTLSNVSERK DNMRLGLSLA TNPKDNSFLA
CSPLWSHECG SSYYTTGMCS RVNSNFRFSK TVAPALQRCQ TYMDIVIVLD GSNSIYPWVE
VQHFLINILK KFYIGPGQIQ VGVVQYGEDV VHEFHLNDYR SVKDVVEAAS HIEQRGGTET
RTAFGIEFAR SEAFQKGGRK GAKKVMIVIT DGESHDSPDL EKVIQQSERD NVTRYAVAVL
GYYNRRGINP ETFLNEIKYI ASDPDDKHFF NVTDEAALKD IVDALGDRIF SLEGTNKNET
SFGLEMSQTG FSSHVVEDGV LLGAVGAYDW NGAVLKETSA GKVIPLRESY LKEFPEELKN
HGAYLGYTVT SVVSSRQGRV YVAGAPRFNH TGKVILFTMH NNRSLTIHQA MRGQQIGSYF
GSEITSVDID GDGVTDVLLV GAPMYFNEGR ERGKVYVYEL RQNLFVYNGT LKDSHSYQNA
RFGSSIASVR DLNQDSYNDV VVGAPLEDNH AGAIYIFHGF RGSILKTPKQ RITASELATG
LQYFGCSIHG QLDLNEDGLI DLAVGALGNA VILWSRPVVQ INASLHFEPS KINIFHRDCK
RSGRDATCLA AFLCFTPIFL APHFQTTTVG IRYNATMDER RYTPRAHLDE GGDRFTNRAV
LLSSGQELCE RINFHVLDTA DYVKPVTFSV EYSLEDPDHG PMLDDGWPTT LRVSVPFWNG
CNEDEHCVPD LVLDARSDLP TAMEYCQRVL RKPAQDCSAY TLSFDTTVFI IESTRQRVAV
EATLENRGEN AYSTVLNISQ SANLQFASLI QKEDSDGSIE CVNEERRLQK QVCNVSYPFF
RAKAKVAFRL DFEFSKSIFL HHLEIELAAG SDSNERDSTK EDNVAPLRFH LKYEADVLFT
RSSSLSHYEV KPNSSLERYD GIGPPFSCIF RIQNLGLFPI HGMMMKITIP IATRSGNRLL
KLRDFLTDEA NTSCNIWGNS TEYRPTPVEE DLRRAPQLNH SNSDVVSINC NIRLVPNQEI
NFHLLGNLWL RSLKALKYKS MKIMVNAALQ RQFHSPFIFR EEDPSRQIVF EISKQEDWQV
PIWIIVGSTL GGLLLLALLV LALWKLGFFR SARRRREPGL DPTPKVLE
