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 27-MAR-2024, entry version 165. 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 a 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 a component of CC the EARP complex that is involved in endocytic recycling. The EARP CC complex associates with Rab4-positive endosomes and promotes recycling CC of 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 (via N-terminus) CC (PubMed:20685960). Interacts with VPS50 and VPS54 in an EIPR1- CC independent manner (PubMed:31721635). {ECO:0000269|PubMed:20685960, CC ECO:0000269|PubMed:25799061, ECO:0000269|PubMed:27440922, CC ECO:0000269|PubMed:30624672, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 186. DR ComplexPortal; CPX-6207; EARP tethering complex. DR ComplexPortal; CPX-6208; GARP tethering complex. DR CORUM; Q9UID3; -. DR DIP; DIP-60562N; -. DR IntAct; Q9UID3; 40. 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; 9606-ENSP00000279281; -. DR PeptideAtlas; Q9UID3; -. DR ProteomicsDB; 84494; -. [Q9UID3-1] DR ProteomicsDB; 84495; -. [Q9UID3-2] DR Pumba; Q9UID3; -. DR Antibodypedia; 49945; 99 antibodies from 27 providers. DR DNASU; 738; -. DR Ensembl; ENST00000279281.8; ENSP00000279281.3; ENSG00000149823.10. [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 AGR; HGNC:1172; -. 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; HRCLEPV; -. DR OrthoDB; 277063at2759; -. 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; 436 hits in 1169 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 197 other cell types or tissues. DR ExpressionAtlas; Q9UID3; baseline and differential. 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:HPA. 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:0007041; P:lysosomal transport; IMP:MGI. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB. DR GO; GO:0090119; P:vesicle-mediated cholesterol transport; IEA:Ensembl. DR InterPro; IPR016159; Cullin_repeat-like_dom_sf. DR InterPro; IPR014812; Vps51. DR PANTHER; PTHR15954; UNCHARACTERIZED; 1. DR PANTHER; PTHR15954:SF4; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 51 HOMOLOG; 1. DR Pfam; PF08700; VPS51_Exo84_N; 1. DR SUPFAM; SSF74788; Cullin repeat-like; 1. DR Genevisible; Q9UID3; HS. 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; uncertain 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 //