AMOT_HUMAN
ID AMOT_HUMAN Reviewed; 1084 AA.
AC Q4VCS5; Q504X5; Q9HD27; Q9UPT1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Angiomotin;
GN Name=AMOT; Synonyms=KIAA1071;
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), TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=11257124; DOI=10.1083/jcb.152.6.1247;
RA Troyanovsky B., Levchenko T., Maensson G., Matvijenko O., Holmgren L.;
RT "Angiomotin. An angiostatin binding protein that regulates endothelial cell
RT migration and tube formation.";
RL J. Cell Biol. 152:1247-1254(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TOPOLOGY, INTERACTION WITH
RP ANGIOSTATIN AND MAGI1, AND SUBCELLULAR LOCATION.
RX PubMed=16043488; DOI=10.1074/jbc.m503915200;
RA Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M.,
RA Holmgren L.;
RT "Angiomotin regulates endothelial cell-cell junctions and cell motility.";
RL J. Biol. Chem. 280:34859-34869(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543 (ISOFORM 1).
RC TISSUE=Spinal cord;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, FUNCTION, AND IDENTIFICATION
RP IN A COMPLEX WITH ARHGAP17; PALS1; PATJ AND PARD3.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP UBIQUITINATION BY NEDD4; NEDD4L AND ITCH.
RX PubMed=22385262; DOI=10.1042/bj20111983;
RA Wang C., An J., Zhang P., Xu C., Gao K., Wu D., Wang D., Yu H., Liu J.O.,
RA Yu L.;
RT "The Nedd4-like ubiquitin E3 ligases target angiomotin/p130 to ubiquitin-
RT dependent degradation.";
RL Biochem. J. 444:279-289(2012).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-594 AND LYS-595, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
CC -!- FUNCTION: Plays a central role in tight junction maintenance via the
CC complex formed with ARHGAP17, which acts by regulating the uptake of
CC polarity proteins at tight junctions. Appears to regulate endothelial
CC cell migration and tube formation. May also play a role in the assembly
CC of endothelial cell-cell junctions. {ECO:0000269|PubMed:11257124,
CC ECO:0000269|PubMed:16678097}.
CC -!- SUBUNIT: Component of a complex whose core is composed of ARHGAP17,
CC AMOT, PALS1, PATJ and PARD3/PAR3. Interacts with MAGI1. Isoform 1
CC interacts with angiostatin. {ECO:0000269|PubMed:16043488,
CC ECO:0000269|PubMed:16678097}.
CC -!- INTERACTION:
CC Q4VCS5; Q68EM7: ARHGAP17; NbExp=2; IntAct=EBI-2511319, EBI-1642807;
CC Q4VCS5; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-2511319, EBI-81279;
CC Q4VCS5; P35240: NF2; NbExp=9; IntAct=EBI-2511319, EBI-1014472;
CC Q4VCS5; P46662: Nf2; Xeno; NbExp=2; IntAct=EBI-2511319, EBI-644586;
CC Q4VCS5; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-2511319, EBI-25492395;
CC Q4VCS5-1; P35240: NF2; NbExp=2; IntAct=EBI-3903812, EBI-1014472;
CC Q4VCS5-2; Q68EM7: ARHGAP17; NbExp=4; IntAct=EBI-3891843, EBI-1642807;
CC Q4VCS5-2; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-3891843, EBI-747505;
CC Q4VCS5-2; P19012: KRT15; NbExp=3; IntAct=EBI-3891843, EBI-739566;
CC Q4VCS5-2; Q15323: KRT31; NbExp=3; IntAct=EBI-3891843, EBI-948001;
CC Q4VCS5-2; P61968: LMO4; NbExp=3; IntAct=EBI-3891843, EBI-2798728;
CC Q4VCS5-2; Q96LR2: LURAP1; NbExp=3; IntAct=EBI-3891843, EBI-741355;
CC Q4VCS5-2; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-3891843, EBI-10194128;
CC Q4VCS5-2; Q9NPJ6: MED4; NbExp=3; IntAct=EBI-3891843, EBI-394607;
CC Q4VCS5-2; P35240: NF2; NbExp=6; IntAct=EBI-3891843, EBI-1014472;
CC Q4VCS5-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-3891843, EBI-741158;
CC Q4VCS5-2; Q13526: PIN1; NbExp=3; IntAct=EBI-3891843, EBI-714158;
CC Q4VCS5-2; Q15257: PTPA; NbExp=3; IntAct=EBI-3891843, EBI-1774121;
CC Q4VCS5-2; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-3891843, EBI-693002;
CC Q4VCS5-2; O75971: SNAPC5; NbExp=3; IntAct=EBI-3891843, EBI-749483;
CC Q4VCS5-2; Q13432: UNC119; NbExp=3; IntAct=EBI-3891843, EBI-711260;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:16043488}. Note=Localized on the cell surface. May
CC act as a transmembrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=p130;
CC IsoId=Q4VCS5-1; Sequence=Displayed;
CC Name=2; Synonyms=p80;
CC IsoId=Q4VCS5-2; Sequence=VSP_015709;
CC -!- TISSUE SPECIFICITY: Expressed in placenta and skeletal muscle. Found in
CC the endothelial cells of capillaries as well as larger vessels of the
CC placenta. {ECO:0000269|PubMed:11257124}.
CC -!- DOMAIN: The coiled coil domain interacts directly with the BAR domain
CC of ARHGAP17. {ECO:0000269|PubMed:16678097}.
CC -!- DOMAIN: The angiostatin binding domain (871-1005) allows the binding to
CC angiostatin. {ECO:0000269|PubMed:16678097}.
CC -!- PTM: Polyubiquitinated by NEDD4, NEDD4L and ITCH, leading to
CC proteasomal degradation. {ECO:0000269|PubMed:22385262}.
CC -!- MISCELLANEOUS: 'Motus' means 'motility' in Latin.
CC -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94712.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AMOTID632chXq23.html";
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DR EMBL; AF286598; AAG01851.1; -; mRNA.
DR EMBL; AY987378; AAY24451.1; -; mRNA.
DR EMBL; AB028994; BAA83023.3; -; mRNA.
DR EMBL; BC094712; AAH94712.1; ALT_SEQ; mRNA.
DR CCDS; CCDS14563.1; -. [Q4VCS5-2]
DR CCDS; CCDS48154.1; -. [Q4VCS5-1]
DR RefSeq; NP_001106962.1; NM_001113490.1. [Q4VCS5-1]
DR RefSeq; NP_573572.1; NM_133265.2. [Q4VCS5-2]
DR RefSeq; XP_005262144.1; XM_005262087.1. [Q4VCS5-1]
DR RefSeq; XP_005262147.1; XM_005262090.1. [Q4VCS5-2]
DR RefSeq; XP_011529177.1; XM_011530875.2. [Q4VCS5-1]
DR RefSeq; XP_016884778.1; XM_017029289.1. [Q4VCS5-2]
DR PDB; 6JJX; X-ray; 2.00 A; C/D=272-293.
DR PDB; 7LP2; X-ray; 1.88 A; B/D/F=233-247.
DR PDB; 7LP3; X-ray; 1.61 A; B/D=234-247.
DR PDB; 7LP5; NMR; -; A=100-114.
DR PDB; 7NMA; X-ray; 1.75 A; P=169-181.
DR PDB; 7NMW; X-ray; 1.50 A; P=169-181.
DR PDB; 7NMX; X-ray; 2.30 A; P=169-181.
DR PDB; 7NN2; X-ray; 1.80 A; P=169-181.
DR PDB; 7NND; X-ray; 1.40 A; P=169-181.
DR PDB; 7NNE; X-ray; 1.96 A; P=169-181.
DR PDB; 7NP2; X-ray; 1.27 A; P=169-188.
DR PDB; 7NPB; X-ray; 1.37 A; P=169-188.
DR PDB; 7NPG; X-ray; 1.37 A; P=169-188.
DR PDBsum; 6JJX; -.
DR PDBsum; 7LP2; -.
DR PDBsum; 7LP3; -.
DR PDBsum; 7LP5; -.
DR PDBsum; 7NMA; -.
DR PDBsum; 7NMW; -.
DR PDBsum; 7NMX; -.
DR PDBsum; 7NN2; -.
DR PDBsum; 7NND; -.
DR PDBsum; 7NNE; -.
DR PDBsum; 7NP2; -.
DR PDBsum; 7NPB; -.
DR PDBsum; 7NPG; -.
DR AlphaFoldDB; Q4VCS5; -.
DR SMR; Q4VCS5; -.
DR BioGRID; 127557; 283.
DR CORUM; Q4VCS5; -.
DR DIP; DIP-53711N; -.
DR ELM; Q4VCS5; -.
DR IntAct; Q4VCS5; 105.
DR MINT; Q4VCS5; -.
DR STRING; 9606.ENSP00000361027; -.
DR ChEMBL; CHEMBL3392949; -.
DR GlyGen; Q4VCS5; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q4VCS5; -.
DR PhosphoSitePlus; Q4VCS5; -.
DR BioMuta; AMOT; -.
DR DMDM; 74753814; -.
DR EPD; Q4VCS5; -.
DR jPOST; Q4VCS5; -.
DR MassIVE; Q4VCS5; -.
DR MaxQB; Q4VCS5; -.
DR PaxDb; Q4VCS5; -.
DR PeptideAtlas; Q4VCS5; -.
DR PRIDE; Q4VCS5; -.
DR ProteomicsDB; 62307; -. [Q4VCS5-1]
DR ProteomicsDB; 62308; -. [Q4VCS5-2]
DR Antibodypedia; 29579; 455 antibodies from 31 providers.
DR DNASU; 154796; -.
DR Ensembl; ENST00000304758.5; ENSP00000305557.1; ENSG00000126016.17. [Q4VCS5-2]
DR Ensembl; ENST00000371959.9; ENSP00000361027.3; ENSG00000126016.17. [Q4VCS5-1]
DR GeneID; 154796; -.
DR KEGG; hsa:154796; -.
DR MANE-Select; ENST00000371959.9; ENSP00000361027.3; NM_001113490.2; NP_001106962.1.
DR UCSC; uc004epr.4; human. [Q4VCS5-1]
DR CTD; 154796; -.
DR DisGeNET; 154796; -.
DR GeneCards; AMOT; -.
DR HGNC; HGNC:17810; AMOT.
DR HPA; ENSG00000126016; Tissue enhanced (epididymis, tongue).
DR MIM; 300410; gene.
DR neXtProt; NX_Q4VCS5; -.
DR OpenTargets; ENSG00000126016; -.
DR PharmGKB; PA24773; -.
DR VEuPathDB; HostDB:ENSG00000126016; -.
DR eggNOG; ENOG502QVI5; Eukaryota.
DR GeneTree; ENSGT00940000159055; -.
DR InParanoid; Q4VCS5; -.
DR OMA; NLGPQSD; -.
DR OrthoDB; 369983at2759; -.
DR PhylomeDB; Q4VCS5; -.
DR TreeFam; TF333368; -.
DR PathwayCommons; Q4VCS5; -.
DR Reactome; R-HSA-2028269; Signaling by Hippo. [Q4VCS5-1]
DR SignaLink; Q4VCS5; -.
DR SIGNOR; Q4VCS5; -.
DR BioGRID-ORCS; 154796; 9 hits in 696 CRISPR screens.
DR ChiTaRS; AMOT; human.
DR GeneWiki; AMOT; -.
DR GenomeRNAi; 154796; -.
DR Pharos; Q4VCS5; Tbio.
DR PRO; PR:Q4VCS5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q4VCS5; protein.
DR Bgee; ENSG00000126016; Expressed in middle frontal gyrus and 111 other tissues.
DR ExpressionAtlas; Q4VCS5; baseline and differential.
DR Genevisible; Q4VCS5; HS.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0043532; F:angiostatin binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
DR GO; GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IBA:GO_Central.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0035329; P:hippo signaling; IGI:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; TAS:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; TAS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR InterPro; IPR009114; Angiomotin.
DR InterPro; IPR024646; Angiomotin_C.
DR Pfam; PF12240; Angiomotin_C; 1.
DR PRINTS; PR01807; ANGIOMOTIN.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Coiled coil;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Tight junction;
KW Ubl conjugation.
FT CHAIN 1..1084
FT /note="Angiomotin"
FT /id="PRO_0000190668"
FT REGION 24..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..689
FT /evidence="ECO:0000255"
FT COILED 721..751
FT /evidence="ECO:0000255"
FT MOTIF 1081..1084
FT /note="PDZ-binding"
FT COMPBIAS 24..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHG2"
FT CROSSLNK 594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 595
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:11257124"
FT /id="VSP_015709"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:7LP5"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:7LP3"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:7LP3"
SQ SEQUENCE 1084 AA; 118085 MW; D7E7021E9535A628 CRC64;
MRNSEEQPSG GTTVLQRLLQ EQLRYGNPSE NRSLLAIHQQ ATGNGPPFPS GSGNPGPQSD
VLSPQDHHQQ LVAHAARQEP QGQEIQSENL IMEKQLSPRM QNNEELPTYE EAKVQSQYFR
GQQHASVGAA FYVTGVTNQK MRTEGRPSVQ RLNPGKMHQD EGLRDLKQGH VRSLSERLMQ
MSLATSGVKA HPPVTSAPLS PPQPNDLYKN PTSSSEFYKA QGPLPNQHSL KGMEHRGPPP
EYPFKGMPPQ SVVCKPQEPG HFYSEHRLNQ PGRTEGQLMR YQHPPEYGAA RPAQDISLPL
SARNSQPHSP TSSLTSGGSL PLLQSPPSTR LSPARHPLVP NQGDHSAHLP RPQQHFLPNQ
AHQGDHYRLS QPGLSQQQQQ QQQQHHHHHH HQQQQQQQPQ QQPGEAYSAM PRAQPSSASY
QPVPADPFAI VSRAQQMVEI LSDENRNLRQ ELEGCYEKVA RLQKVETEIQ RVSEAYENLV
KSSSKREALE KAMRNKLEGE IRRMHDFNRD LRERLETANK QLAEKEYEGS EDTRKTISQL
FAKNKESQRE KEKLEAELAT ARSTNEDQRR HIEIRDQALS NAQAKVVKLE EELKKKQVYV
DKVEKMQQAL VQLQAACEKR EQLEHRLRTR LERELESLRI QQRQGNCQPT NVSEYNAAAL
MELLREKEER ILALEADMTK WEQKYLEENV MRHFALDAAA TVAAQRDTTV ISHSPNTSYD
TALEARIQKE EEEILMANKR CLDMEGRIKT LHAQIIEKDA MIKVLQQRSR KEPSKTEQLS
CMRPAKSLMS ISNAGSGLLS HSSTLTGSPI MEEKRDDKSW KGSLGILLGG DYRAEYVPST
PSPVPPSTPL LSAHSKTGSR DCSTQTERGT ESNKTAAVAP ISVPAPVAAA ATAAAITATA
ATITTTMVAA APVAVAAAAA PAAAAAPSPA TAAATAAAVS PAAAGQIPAA ASVASAAAVA
PSAAAAAAVQ VAPAAPAPVP APALVPVPAP AAAQASAPAQ TQAPTSAPAV APTPAPTPTP
AVAQAEVPAS PATGPGPHRL SIPSLTCNPD KTDGPVFHSN TLERKTPIQI LGQEPDAEMV
EYLI
