VPS51_HUMAN
ID VPS51_HUMAN Reviewed; 782 AA.
AC Q9UID3; Q6PJV5; Q7L8A6; Q8WZ35; Q96DF4; Q96GR3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Vacuolar protein sorting-associated protein 51 homolog;
DE AltName: Full=Another new gene 2 protein;
DE AltName: Full=Protein fat-free homolog;
GN Name=VPS51; Synonyms=ANG2, C11orf2, C11orf3, FFR; ORFNames=PP5382;
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 1).
RX PubMed=9615229; DOI=10.1006/geno.1998.5296;
RA Lemmens I.H., Kas K., Merregaert J., Van de Ven W.J.M.;
RT "Identification and molecular characterization of TM7SF2 in the FAUNA gene
RT cluster on human chromosome 11q13.";
RL Genomics 49:437-442(1998).
RN [2]
RP SEQUENCE REVISION.
RA Lemmens I.H., Kas K., Merregaert J., Van de Ven W.J.M.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, Eye, Lung, and Muscle;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-782 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS52; VPS53; VPS54
RP AND STX6.
RX PubMed=20685960; DOI=10.1091/mbc.e10-05-0392;
RA Perez-Victoria F.J., Schindler C., Magadan J.G., Mardones G.A.,
RA Delevoye C., Romao M., Raposo G., Bonifacino J.S.;
RT "Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde
RT protein complex.";
RL Mol. Biol. Cell 21:3386-3395(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-649, AND
RP IDENTIFICATION BY 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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE EARP COMPLEX.
RX PubMed=25799061; DOI=10.1038/ncb3129;
RA Schindler C., Chen Y., Pu J., Guo X., Bonifacino J.S.;
RT "EARP is a multisubunit tethering complex involved in endocytic
RT recycling.";
RL Nat. Cell Biol. 17:639-650(2015).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP INTERACTION WITH EIPR1, IDENTIFICATION IN THE EARP COMPLEX, AND
RP IDENTIFICATION IN THE GARP COMPLEX.
RX PubMed=27440922; DOI=10.1091/mbc.e16-04-0209;
RA Gershlick D.C., Schindler C., Chen Y., Bonifacino J.S.;
RT "TSSC1 is novel component of the endosomal retrieval machinery.";
RL Mol. Biol. Cell 27:2867-2878(2016).
RN [17]
RP INTERACTION WITH VPS50 AND VPS54.
RX PubMed=31721635; DOI=10.1091/mbc.e18-07-0469;
RA Topalidou I., Cattin-Ortola J., Hummer B., Asensio C.S., Ailion M.;
RT "EIPR1 controls dense-core vesicle cargo retention and EARP complex
RT localization in insulin-secreting cells.";
RL Mol. Biol. Cell 31:59-79(2020).
RN [18]
RP VARIANT PCH13 CYS-490, INVOLVEMENT IN PCH13, CHARACTERIZATION OF VARIANT
RP PCH13 CYS-490, AND INTERACTION WITH VSP50 AND VSP53.
RX PubMed=30624672; DOI=10.1093/hmg/ddy423;
RA Gershlick D.C., Ishida M., Jones J.R., Bellomo A., Bonifacino J.S.,
RA Everman D.B.;
RT "A neurodevelopmental disorder caused by mutations in the VPS51 subunit of
RT the GARP and EARP complexes.";
RL Hum. Mol. Genet. 28:1548-1560(2019).
RN [19]
RP VARIANT PCH13 PHE-474 DEL, AND INVOLVEMENT IN PCH13.
RX PubMed=31207318; DOI=10.1016/j.ejmg.2019.103704;
RA Uwineza A., Caberg J.H., Hitayezu J., Wenric S., Mutesa L., Vial Y.,
RA Drunat S., Passemard S., Verloes A., El Ghouzzi V., Bours V.;
RT "VPS51 biallelic variants cause microcephaly with brain malformations: A
RT confirmatory report.";
RL Eur. J. Med. Genet. 62:103704-103704(2019).
CC -!- FUNCTION: Acts as component of the GARP complex that is involved in
CC retrograde transport from early and late endosomes to the trans-Golgi
CC network (TGN). The GARP complex is required for the maintenance of
CC protein retrieval from endosomes to the TGN, acid hydrolase sorting,
CC lysosome function, endosomal cholesterol traffic and autophagy. VPS51
CC participates in retrograde transport of acid hydrolase receptors,
CC likely by promoting tethering and SNARE-dependent fusion of endosome-
CC derived carriers to the TGN (PubMed:20685960). Acts as component of the
CC EARP complex that is involved in endocytic recycling. The EARP complex
CC associates with Rab4-positive endosomes and promotes recycling of
CC internalized transferrin receptor (TFRC) to the plasma membrane
CC (PubMed:25799061). {ECO:0000269|PubMed:20685960,
CC ECO:0000269|PubMed:25799061}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, also called VFT (VPS fifty-three) complex, composed of VPS51,
CC VPS52, VPS53 and VPS54 (PubMed:20685960, PubMed:27440922,
CC PubMed:30624672). Component of the endosome-associated retrograde
CC protein (EARP) complex, composed of VPS51, VPS52, VPS53 and
CC VPS50/Syndetin (PubMed:25799061, PubMed:27440922, PubMed:30624672).
CC EIPR1 interacts with both EARP and GARP complexes and mediates the
CC recruitment of the GARP complex to the trans-Golgi network
CC (PubMed:27440922). Interacts with STX6 (PubMed:20685960). Interacts
CC with VPS50 and VPS54 in an EIPR1-independent manner (PubMed:31721635).
CC {ECO:0000269|PubMed:20685960, ECO:0000269|PubMed:25799061,
CC ECO:0000269|PubMed:27440922, ECO:0000269|PubMed:30624672,
CC ECO:0000269|PubMed:31721635}.
CC -!- INTERACTION:
CC Q9UID3-1; O60499-1: STX10; NbExp=5; IntAct=EBI-16067837, EBI-16067850;
CC Q9UID3-1; O43752: STX6; NbExp=8; IntAct=EBI-16067837, EBI-2695795;
CC Q9UID3-1; Q96JG6: VPS50; NbExp=6; IntAct=EBI-16067837, EBI-11044388;
CC Q9UID3-1; Q8N1B4: VPS52; NbExp=4; IntAct=EBI-16067837, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:20685960}. Recycling endosome
CC {ECO:0000269|PubMed:25799061}. Note=Localizes to the trans-Golgi
CC network as part of the GARP complex, while it localizes to recycling
CC endosomes as part of the EARP complex (PubMed:25799061).
CC {ECO:0000269|PubMed:25799061}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UID3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UID3-2; Sequence=VSP_014700;
CC -!- DISEASE: Pontocerebellar hypoplasia 13 (PCH13) [MIM:618606]: A form of
CC pontocerebellar hypoplasia, a disorder characterized by structural
CC defects of the pons and cerebellum, evident upon brain imaging. PCH13
CC is an autosomal recessive form characterized by delayed psychomotor
CC development, absent speech, severe intellectual disability and
CC postnatal microcephaly, with brain malformations consisting of
CC cerebellar atrophy and hypoplastic corpus callosum. Additional
CC features, including seizures and visual impairment, are variable.
CC {ECO:0000269|PubMed:30624672, ECO:0000269|PubMed:31207318}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
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DR EMBL; AF024631; AAF21627.2; -; mRNA.
DR EMBL; AF289557; AAL55741.1; -; mRNA.
DR EMBL; AL833818; CAD38681.2; -; mRNA.
DR EMBL; AP003068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006555; AAH06555.2; -; mRNA.
DR EMBL; BC007198; AAH07198.1; -; mRNA.
DR EMBL; BC009285; AAH09285.2; -; mRNA.
DR EMBL; BC010540; AAH10540.1; -; mRNA.
DR EMBL; BC017438; AAH17438.1; -; mRNA.
DR CCDS; CCDS8093.1; -. [Q9UID3-1]
DR RefSeq; NP_037397.2; NM_013265.3. [Q9UID3-1]
DR PDB; 4J2C; X-ray; 1.80 A; B/D=33-49.
DR PDBsum; 4J2C; -.
DR AlphaFoldDB; Q9UID3; -.
DR SMR; Q9UID3; -.
DR BioGRID; 107197; 173.
DR ComplexPortal; CPX-6207; EARP tethering complex.
DR ComplexPortal; CPX-6208; GARP tethering complex.
DR CORUM; Q9UID3; -.
DR DIP; DIP-60562N; -.
DR IntAct; Q9UID3; 38.
DR MINT; Q9UID3; -.
DR STRING; 9606.ENSP00000279281; -.
DR GlyGen; Q9UID3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UID3; -.
DR PhosphoSitePlus; Q9UID3; -.
DR BioMuta; VPS51; -.
DR DMDM; 71153003; -.
DR EPD; Q9UID3; -.
DR jPOST; Q9UID3; -.
DR MassIVE; Q9UID3; -.
DR MaxQB; Q9UID3; -.
DR PaxDb; Q9UID3; -.
DR PeptideAtlas; Q9UID3; -.
DR PRIDE; Q9UID3; -.
DR ProteomicsDB; 84494; -. [Q9UID3-1]
DR ProteomicsDB; 84495; -. [Q9UID3-2]
DR Antibodypedia; 49945; 86 antibodies from 26 providers.
DR DNASU; 738; -.
DR Ensembl; ENST00000279281.8; ENSP00000279281.3; ENSG00000149823.9. [Q9UID3-1]
DR GeneID; 738; -.
DR KEGG; hsa:738; -.
DR MANE-Select; ENST00000279281.8; ENSP00000279281.3; NM_013265.4; NP_037397.2.
DR UCSC; uc001ocr.3; human. [Q9UID3-1]
DR CTD; 738; -.
DR DisGeNET; 738; -.
DR GeneCards; VPS51; -.
DR HGNC; HGNC:1172; VPS51.
DR HPA; ENSG00000149823; Low tissue specificity.
DR MalaCards; VPS51; -.
DR MIM; 615738; gene.
DR MIM; 618606; phenotype.
DR neXtProt; NX_Q9UID3; -.
DR OpenTargets; ENSG00000149823; -.
DR PharmGKB; PA25485; -.
DR VEuPathDB; HostDB:ENSG00000149823; -.
DR eggNOG; KOG2346; Eukaryota.
DR GeneTree; ENSGT00390000001738; -.
DR HOGENOM; CLU_020677_0_0_1; -.
DR InParanoid; Q9UID3; -.
DR OMA; HTIEPRT; -.
DR OrthoDB; 1305393at2759; -.
DR PhylomeDB; Q9UID3; -.
DR TreeFam; TF314825; -.
DR PathwayCommons; Q9UID3; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q9UID3; -.
DR BioGRID-ORCS; 738; 424 hits in 1084 CRISPR screens.
DR ChiTaRS; VPS51; human.
DR GenomeRNAi; 738; -.
DR Pharos; Q9UID3; Tbio.
DR PRO; PR:Q9UID3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UID3; protein.
DR Bgee; ENSG00000149823; Expressed in body of pancreas and 195 other tissues.
DR ExpressionAtlas; Q9UID3; baseline and differential.
DR Genevisible; Q9UID3; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:1990745; C:EARP complex; IDA:UniProtKB.
DR GO; GO:0000938; C:GARP complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007041; P:lysosomal transport; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR InterPro; IPR014812; Vps51.
DR PANTHER; PTHR15954; PTHR15954; 1.
DR Pfam; PF15469; Sec5; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Disease variant; Endosome; Golgi apparatus; Intellectual disability;
KW Lipid transport; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..782
FT /note="Vacuolar protein sorting-associated protein 51
FT homolog"
FT /id="PRO_0000089831"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..147
FT /evidence="ECO:0000255"
FT COILED 270..292
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UVL4"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_014700"
FT VARIANT 474
FT /note="Missing (in PCH13; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31207318"
FT /id="VAR_083138"
FT VARIANT 490
FT /note="R -> C (in PCH13; impaired association with VPS50
FT and VPS53 subunits; reduced levels of assembled GARP and
FT EARP complexes; dbSNP:rs1203009966)"
FT /evidence="ECO:0000269|PubMed:30624672"
FT /id="VAR_083139"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:4J2C"
SQ SEQUENCE 782 AA; 86042 MW; 0E858672E4C656DD CRC64;
MAAAAAAGPS PGSGPGDSPE GPEGEAPERR RKAHGMLKLY YGLSEGEAAG RPAGPDPLDP
TDLNGAHFDP EVYLDKLRRE CPLAQLMDSE TDMVRQIRAL DSDMQTLVYE NYNKFISATD
TIRKMKNDFR KMEDEMDRLA TNMAVITDFS ARISATLQDR HERITKLAGV HALLRKLQFL
FELPSRLTKC VELGAYGQAV RYQGRAQAVL QQYQHLPSFR AIQDDCQVIT ARLAQQLRQR
FREGGSGAPE QAECVELLLA LGEPAEELCE EFLAHARGRL EKELRNLEAE LGPSPPAPDV
LEFTDHGGSG FVGGLCQVAA AYQELFAAQG PAGAEKLAAF ARQLGSRYFA LVERRLAQEQ
GGGDNSLLVR ALDRFHRRLR APGALLAAAG LADAATEIVE RVARERLGHH LQGLRAAFLG
CLTDVRQALA APRVAGKEGP GLAELLANVA SSILSHIKAS LAAVHLFTAK EVSFSNKPYF
RGEFCSQGVR EGLIVGFVHS MCQTAQSFCD SPGEKGGATP PALLLLLSRL CLDYETATIS
YILTLTDEQF LVQDQFPVTP VSTLCAEARE TARRLLTHYV KVQGLVISQM LRKSVETRDW
LSTLEPRNVR AVMKRVVEDT TAIDVQVGLL YEEGVRKAQS SDSSKRTFSV YSSSRQQGRY
APSYTPSAPM DTNLLSNIQK LFSERIDVFS PVEFNKVSVL TGIIKISLKT LLECVRLRTF
GRFGLQQVQV DCHFLQLYLW RFVADEELVH LLLDEVVASA ALRCPDPVPM EPSVVEVICE
RG
