ITAV_BOVIN
ID ITAV_BOVIN Reviewed; 1048 AA.
AC P80746; Q0PDN6; Q9GK48; Q9MZD6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Integrin alpha-V;
DE AltName: Full=Vitronectin receptor subunit alpha;
DE AltName: CD_antigen=CD51;
DE Contains:
DE RecName: Full=Integrin alpha-V heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-V light chain;
DE Flags: Precursor;
GN Name=ITGAV;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FMDV CAPSID PROTEINS
RP (MICROBIAL INFECTION).
RC TISSUE=Lung;
RX PubMed=10906183; DOI=10.1128/jvi.74.16.7298-7306.2000;
RA Neff S., Mason P.W., Baxt B.;
RT "High-efficiency utilization of the bovine integrin alpha(v)beta(3) as a
RT receptor for foot-and-mouth disease virus is dependent on the bovine
RT beta(3) subunit.";
RL J. Virol. 74:7298-7306(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Du J., Chang H., Cong G., Shao J., Lin T., Liu Z., Liu X., Cai X., Xie Q.;
RT "Molecular cloning and characteristics of bovine alpha V cDNA.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-1048.
RC TISSUE=Mammary gland;
RA Andersen M.H., Rasmussen J.T., Berglund L., Petersen T.E.;
RT "Bovine alpha-V integrin subunit (fragment).";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 31-50 AND 891-910.
RC TISSUE=Mammary gland;
RX PubMed=9154926; DOI=10.1021/bi963119m;
RA Andersen M.H., Berglund L., Rasmussen J.T., Petersen T.E.;
RT "Bovine PAS-6/7 binds alpha v beta 5 integrins and anionic phospholipids
RT through two domains.";
RL Biochemistry 36:5441-5446(1997).
RN [5]
RP INTERACTION WITH HOST FMDV VP1 (MICROBIAL INFECTION).
RX PubMed=12551988; DOI=10.1128/jvi.77.4.2500-2511.2003;
RA Duque H., Baxt B.;
RT "Foot-and-mouth disease virus receptors: comparison of bovine alpha(V)
RT integrin utilization by type A and O viruses.";
RL J. Virol. 77:2500-2511(2003).
CC -!- FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin,
CC cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-
CC 2, osteopontin, osteomodulin, prothrombin, thrombospondin, TGFB1 and
CC vWF. They recognize the sequence R-G-D in a wide array of ligands.
CC Alpha-V integrins may play a role in embryo implantation, angiogenesis
CC and wound healing (By similarity). ITGAV:ITGB3 binds to fractalkine
CC (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine
CC signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding
CC is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and
CC this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2
CC and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to
CC IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3
CC binds to IGF2 and this binding is essential for IGF2 signaling.
CC ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B
CC signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is
CC distinct from the classical ligand-binding site (site 1) and this
CC induces integrin conformational changes and enhanced ligand binding to
CC site 1. ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for fibrillin-1
CC (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (By
CC similarity). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or
CC ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth
CC factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide
CC (LAP), thereby playing a key role in TGF-beta-1 activation (By
CC similarity). ITGAV:ITGB3 acts as a receptor for CD40LG (By similarity).
CC {ECO:0000250|UniProtKB:P06756, ECO:0000250|UniProtKB:P43406}.
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-V (ITGAV) associates with either beta-1 (ITGB1), beta-3 (ITGB3),
CC beta-5 (ITGB5), beta-6 (ITGB6) or beta-8 (ITGB8) (By similarity).
CC Interacts with RAB25. Interacts with CIB1 (By similarity). Integrins
CC ITGAV:ITGB3 and ITGAV:ITGB5 interact with FBLN5 (via N-terminus) (By
CC similarity). ITGAV:ITGB3 and ITGAV:ITGB5 interact with CCN3 (By
CC similarity). ITGAV:ITGB3 interacts with ADGRA2 (By similarity).
CC ITGAV:ITGB3 interacts with FGF2; it is likely that FGF2 can
CC simultaneously bind ITGAV:ITGB3 and FGF receptors (By similarity).
CC ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1.
CC ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3.
CC ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1.
CC ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (By
CC similarity). ITGAV:ITGB3 interacts with IGF2 (By similarity).
CC ITGAV:ITGB3 and ITGAV:ITGB6 interact with FBN1 (By similarity).
CC ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second
CC extracellular domain) (By similarity). ITGAV:ITGB6 interacts with TGFB1
CC (By similarity). ITGAV:ITGB3 interacts with PTN. Forms a complex with
CC PTPRZ1 and PTN that stimulates endothelial cell migration through ITGB3
CC 'Tyr-773' phosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:P06756, ECO:0000250|UniProtKB:P43406}.
CC -!- SUBUNIT: (Microbial infection) Alpha-V/beta-6 and alpha-V/beta-3 bind
CC to foot-and-mouth disease virus (FMDV) VP1 protein and acts as a
CC receptor for this virus. {ECO:0000269|PubMed:10906183,
CC ECO:0000269|PubMed:12551988}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P06756}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AF239958; AAF44691.2; -; mRNA.
DR EMBL; DQ871215; ABH07896.1; -; mRNA.
DR EMBL; AF317199; AAG38595.1; -; mRNA.
DR RefSeq; NP_776792.1; NM_174367.1.
DR AlphaFoldDB; P80746; -.
DR SMR; P80746; -.
DR ComplexPortal; CPX-4126; Integrin alphav-beta3 complex.
DR IntAct; P80746; 1.
DR STRING; 9913.ENSBTAP00000026553; -.
DR PaxDb; P80746; -.
DR PeptideAtlas; P80746; -.
DR PRIDE; P80746; -.
DR GeneID; 281875; -.
DR KEGG; bta:281875; -.
DR CTD; 3685; -.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; P80746; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; ISS:UniProtKB.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001568; P:blood vessel development; ISS:AgBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
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; 3.
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; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Integrin; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:9154926"
FT CHAIN 31..1048
FT /note="Integrin alpha-V"
FT /id="PRO_0000016298"
FT CHAIN 31..889
FT /note="Integrin alpha-V heavy chain"
FT /id="PRO_0000016299"
FT CHAIN 891..1048
FT /note="Integrin alpha-V light chain"
FT /id="PRO_0000016300"
FT TOPO_DOM 31..992
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 993..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 32..98
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 109..170
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 173..225
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 237..291
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 292..357
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 358..415
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 419..482
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1027..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1019..1023
FT /note="GFFKR motif"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
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 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..97
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 138..158
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 172..185
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 491..502
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 508..565
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 626..632
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 698..711
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 852..914
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 904..909
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT CONFLICT 12
FT /note="G -> R (in Ref. 2; ABH07896)"
FT /evidence="ECO:0000305"
FT CONFLICT 15..17
FT /note="GLP -> RLL (in Ref. 2; ABH07896)"
FT /evidence="ECO:0000305"
FT CONFLICT 21..23
FT /note="SGL -> PGI (in Ref. 2; ABH07896)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="R -> G (in Ref. 2; ABH07896)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="Missing (in Ref. 1; AAF44691)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="R -> G (in Ref. 3; AAG38595)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="F -> S (in Ref. 2; ABH07896)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="T -> I (in Ref. 2; ABH07896)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="G -> R (in Ref. 1; AAF44691)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="A -> T (in Ref. 1; AAF44691)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="H -> R (in Ref. 1; AAF44691)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="D -> G (in Ref. 1; AAF44691)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="P -> R (in Ref. 3; AAG38595)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="T -> A (in Ref. 3; AAG38595)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="K -> R (in Ref. 1; AAF44691)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="L -> V (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="V -> I (in Ref. 2; ABH07896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1048 AA; 116132 MW; A6A5620EB3144502 CRC64;
MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVESPAE YSGPEGSYFG FAVDFFVPSA
SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSHRRCQPI EFDATGNRDY AKDDPLEFKS
HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSKNIDAD
GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IVSKYDPKVY SIKYNNQLAT
RTAQAIFDDS YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVYIYDGKN MSSLHNFTGE
QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ KASGDFQTIK
LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK GIVYIFNGRP TGLNAVPSQI
LEGKWAARSM PPSFGYSMKG ATDIDKNGYP DLIVGAFGVD RAVLYRARPV ITVNAGLEVY
PSILNQENKT CPLPGTDLKV SCFNVRFCLK ADGKGALPTK LDFQVELLLD KLKQKGAIRR
ALFLHNRSPG HSKNMTISRG GQMQCEELIA YLRDESEFRD KLTPITIFME YWLDYRTAAD
ATGLQPILNQ FTPANVSRQA HILLDCGEDN VCKPKLEVSV DSDQKKIYIG DDNPLTLIVK
AQNQGEGAYE AELIVSIPLQ ADFIGVVRNS EALARLSCAF KTENQTRQVV CDLGNPMKAG
TQLLAGLRFS VHQQSEMDTS VKFDLQIQSS NLFDKVSPVV SYKVDLAVLA AVEIRGVSSP
DHIFLPIPNW KYKENPETEE DVGPVVQHIY ELRNNGPSSF SKAMLHLQWP YKYNNNTLLY
ILQYDIDGPM NCTSDMEINP LRIKISNSQT SEKNDTVGGQ GDRNHLITKR DLTLNEGDVH
TLGCGIAECL KIVCQVGRLD RGKSAILYVR SLLWTETFMN KENQNHSYSL KSSASFNVIE
FPYKNLPIED IFNSTLVTTN VTWGIQPAPM PVPVWVIILA VLAGLLLLAV LVFVMYRMGF
FKRVRPPQEE QEREQLQPHE NGEGNSET
