ITA1_MOUSE
ID ITA1_MOUSE Reviewed; 1179 AA.
AC Q3V3R4; F8VQN5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Integrin alpha-1;
DE AltName: Full=CD49 antigen-like family member A;
DE AltName: Full=Laminin and collagen receptor;
DE AltName: Full=VLA-1;
DE AltName: CD_antigen=CD49a;
DE Flags: Precursor;
GN Name=Itga1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [2]
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 [3]
RP FUNCTION IN EGFR SIGNALING.
RX PubMed=15592458; DOI=10.1038/ncb1209;
RA Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., Ivaska J.;
RT "Negative regulation of EGFR signalling through integrin-alpha1beta1-
RT mediated activation of protein tyrosine phosphatase TCPTP.";
RL Nat. Cell Biol. 7:78-85(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and
CC collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R
CC in collagen. Involved in anchorage-dependent, negative regulation of
CC EGF-stimulated cell growth. {ECO:0000269|PubMed:15592458}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1 associates
CC with beta-1 (By similarity). Interacts with RAB21 (By similarity).
CC Interacts (via cytoplasmic domain) with PTPN2; activates PTPN2
CC phosphatase activity towards EGFR and negatively regulates EGF
CC signaling (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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}.
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DR EMBL; AK035870; BAE20498.1; -; mRNA.
DR EMBL; AC175538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36788.1; -.
DR RefSeq; NP_001028400.2; NM_001033228.3.
DR AlphaFoldDB; Q3V3R4; -.
DR BMRB; Q3V3R4; -.
DR SMR; Q3V3R4; -.
DR BioGRID; 224968; 2.
DR ComplexPortal; CPX-3114; Integrin alpha1-beta1 complex.
DR STRING; 10090.ENSMUSP00000077132; -.
DR GlyConnect; 2395; 6 N-Linked glycans (6 sites).
DR GlyGen; Q3V3R4; 23 sites, 6 N-linked glycans (6 sites).
DR iPTMnet; Q3V3R4; -.
DR PhosphoSitePlus; Q3V3R4; -.
DR SwissPalm; Q3V3R4; -.
DR jPOST; Q3V3R4; -.
DR MaxQB; Q3V3R4; -.
DR PaxDb; Q3V3R4; -.
DR PeptideAtlas; Q3V3R4; -.
DR PRIDE; Q3V3R4; -.
DR ProteomicsDB; 269342; -.
DR Antibodypedia; 10955; 577 antibodies from 38 providers.
DR DNASU; 109700; -.
DR Ensembl; ENSMUST00000061673; ENSMUSP00000077132; ENSMUSG00000042284.
DR GeneID; 109700; -.
DR KEGG; mmu:109700; -.
DR UCSC; uc007rxx.1; mouse.
DR CTD; 3672; -.
DR MGI; MGI:96599; Itga1.
DR VEuPathDB; HostDB:ENSMUSG00000042284; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157646; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; Q3V3R4; -.
DR OMA; THTFLAI; -.
DR OrthoDB; 66046at2759; -.
DR PhylomeDB; Q3V3R4; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 109700; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Itga1; mouse.
DR PRO; PR:Q3V3R4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3V3R4; protein.
DR Bgee; ENSMUSG00000042284; Expressed in right lung and 199 other tissues.
DR Genevisible; Q3V3R4; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; ISO:MGI.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; 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:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0045123; P:cellular extravasation; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; ISO:MGI.
DR Gene3D; 2.130.10.130; -; 1.
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; IPR018184; Integrin_alpha_C_CS.
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; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Magnesium;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..1179
FT /note="Integrin alpha-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273722"
FT TOPO_DOM 29..1141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 30..91
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 101..160
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 175..364
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 365..417
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 422..474
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 475..537
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 556..614
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 618..678
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1167..1171
FT /note="GFFKR motif"
FT BINDING 497
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 583
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
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 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..92
FT /evidence="ECO:0000250"
FT DISULFID 687..696
FT /evidence="ECO:0000250"
FT DISULFID 702..755
FT /evidence="ECO:0000250"
FT DISULFID 807..813
FT /evidence="ECO:0000250"
FT DISULFID 877..885
FT /evidence="ECO:0000250"
FT DISULFID 1029..1062
FT /evidence="ECO:0000250"
FT DISULFID 1065..1072
FT /evidence="ECO:0000250"
FT CONFLICT 782
FT /note="D -> N (in Ref. 1; BAE20498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1179 AA; 130810 MW; D158F297AFA8119F CRC64;
MVPRRPASLE VTVACIWLLT VILGVCISFN VDVKNSMSFS GPVEDMFGYT VQQYENEEGK
WVLIGSPLVG QPKARTGDVY KCPVGRERSM PCVKLDLPVN TSIPNVTEIK ENMTFGSTLV
TNPKGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS FAPVQECSTQ LDIVIVLDGS
NSIYPWESVT AFLNDLLKRM DIGPKQTQVG IVQYGANVTH EFNLNKYSST EEVLVAANKI
GRRGGLQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNYRL KQVIQDCEDE
NIQRFSIAIL GHYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKALGERIF
ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA NQIVIPHNTT
FQTEPTKMNE PLASYLGYTV NSATIPGDVL YIAGQPRYNH TGQVVIYKME DGDVNILQTL
SGEQIGSYFG SVLTTIDIDK DSYTDLLLVG APMYMGTEKE EQGKVYVYAV NQTRFEYQMS
LEPIKQTCCS SLKDNSCTKE NKNEPCGARF GTAVAAVKDL NVDGFNDVVI GAPLEDDHAG
AVYIYHGSGK TIRKEYAQRI PSGGDGKTLK FFGQSIHGEM DLNGDGLTDV TIGGLGGAAL
FWARDVAVVK VTMNFEPNKV NIQKKNCRVE GKETVCINAT MCFHVKLKSK EDSVYEADLQ
YRVTLDSLRQ ISRSFFSGTQ ERRIQRNLTV RESECIRHSF YMLDKHDFQD SVRVTLDFNL
TDPENGPVLD DALPNSVHGH IPFAKDCGNK ERCVSDLTLD VSTTEKNLLI VRSQNDKFNV
SLTVKNKGDS AYNTRTVVQY SPNLIFSGIE EIQKDSCESN QNITCRVGYP FLRTGDVVNF
KIIFQFNTSH LSENAIIHLS ATSDSEEPLE SLYDNEVNIS IPVKYEVGLQ FYSSASEHHI
SVAANETVPE LINSTKDIGD EINVFYTIRK RGHFPMPELR LAISFPNLTS DGYPVLYPTG
WSSSDNVNCR PRSLEDPLGI NSGKKMTISK SEVLKRGTIQ DCSTCKIATI TCHLLPSDVS
QVNVSLILWK PTFIKAHFSS LNLTIRGELQ SENSSLTLSS SNRKRELAIQ ISKDGLPGRV
PLWVILLSAF AGLLLLMLLI LALWKIGFFK RPLKKKMEK
