VPS54_HUMAN
ID VPS54_HUMAN Reviewed; 977 AA.
AC Q9P1Q0; Q5VIR5; Q86YF7; Q8N6G3; Q9NPV0; Q9NT07; Q9NUJ0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Vacuolar protein sorting-associated protein 54;
DE AltName: Full=Hepatocellular carcinoma protein 8;
DE AltName: Full=Tumor antigen HOM-HCC-8;
DE AltName: Full=Tumor antigen SLP-8p;
GN Name=VPS54; Synonyms=HCC8;
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).
RC TISSUE=Hepatoma;
RA Stenner-Liewen F., Luo G., Tuereci O., Sahin U., Liewen H., Koslowski M.,
RA Pfreundschuh M.;
RT "HOM-HCC-8, a novel tumor antigen associated with hepatocellular
RT carcinoma.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RX PubMed=15878329; DOI=10.1016/j.yexcr.2005.01.022;
RA Liewen H., Meinhold-Heerlein I., Oliveira V., Schwarzenbacher R., Luo G.,
RA Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
RT "Characterization of the human GARP (Golgi associated retrograde protein)
RT complex.";
RL Exp. Cell Res. 306:24-34(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Skin, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 579-977.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18367545; DOI=10.1091/mbc.e07-11-1189;
RA Perez-Victoria F.J., Mardones G.A., Bonifacino J.S.;
RT "Requirement of the human GARP complex for mannose 6-phosphate-receptor-
RT dependent sorting of cathepsin D to lysosomes.";
RL Mol. Biol. Cell 19:2350-2362(2008).
RN [7]
RP INTERACTION WITH VPS51.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE GARP 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 [10]
RP IDENTIFICATION IN THE GARP COMPLEX, AND INTERACTION WITH EIPR1.
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 [11]
RP INTERACTION WITH VPS51.
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).
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 the
CC cycling of mannose 6-phosphate receptors between the TGN and endosomes,
CC this cycling is necessary for proper lysosomal sorting of acid
CC hydrolases such as CTSD (PubMed:18367545). Within the GARP complex,
CC required to tether the complex to the TGN. Not involved in endocytic
CC recycling (PubMed:25799061). {ECO:0000269|PubMed:18367545,
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:15878329, PubMed:25799061,
CC PubMed:27440922). EIPR1 interacts with GARP complex and mediates its
CC recruitment to the trans-Golgi network (PubMed:27440922). Interacts
CC with VPS51 in an EIPR1-independent manner (PubMed:31721635).
CC {ECO:0000269|PubMed:15878329, ECO:0000269|PubMed:25799061,
CC ECO:0000269|PubMed:27440922, ECO:0000269|PubMed:31721635}.
CC -!- INTERACTION:
CC Q9P1Q0-4; P55212: CASP6; NbExp=3; IntAct=EBI-25835297, EBI-718729;
CC Q9P1Q0-4; P06307: CCK; NbExp=3; IntAct=EBI-25835297, EBI-6624398;
CC Q9P1Q0-4; P22607: FGFR3; NbExp=3; IntAct=EBI-25835297, EBI-348399;
CC Q9P1Q0-4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-25835297, EBI-8285963;
CC Q9P1Q0-4; P06396: GSN; NbExp=3; IntAct=EBI-25835297, EBI-351506;
CC Q9P1Q0-4; O00291: HIP1; NbExp=3; IntAct=EBI-25835297, EBI-473886;
CC Q9P1Q0-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25835297, EBI-21591415;
CC Q9P1Q0-4; P62826: RAN; NbExp=3; IntAct=EBI-25835297, EBI-286642;
CC Q9P1Q0-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-25835297, EBI-741480;
CC Q9P1Q0-4; Q9Y649; NbExp=3; IntAct=EBI-25835297, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}. Membrane
CC {ECO:0000250|UniProtKB:Q9JMK8}. Note=Associates with membranes in an
CC EIPR1-independent manner. {ECO:0000250|UniProtKB:Q9JMK8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9P1Q0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P1Q0-2; Sequence=VSP_013756;
CC Name=3;
CC IsoId=Q9P1Q0-3; Sequence=VSP_013752, VSP_013754, VSP_013755;
CC Name=4;
CC IsoId=Q9P1Q0-4; Sequence=VSP_013753;
CC Name=5;
CC IsoId=Q9P1Q0-5; Sequence=VSP_013751;
CC -!- SIMILARITY: Belongs to the VPS54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92134.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF102177; AAF37319.1; -; mRNA.
DR EMBL; AY444798; AAS20945.1; -; mRNA.
DR EMBL; AL137604; CAB70837.1; -; mRNA.
DR EMBL; AL359939; CAB95772.1; -; mRNA.
DR EMBL; CR749701; CAH18479.1; -; mRNA.
DR EMBL; BC030275; AAH30275.1; -; mRNA.
DR EMBL; BC041868; AAH41868.1; -; mRNA.
DR EMBL; AK002205; BAA92134.1; ALT_INIT; mRNA.
DR CCDS; CCDS33208.1; -. [Q9P1Q0-1]
DR CCDS; CCDS46302.1; -. [Q9P1Q0-4]
DR PIR; T46308; T46308.
DR RefSeq; NP_001005739.1; NM_001005739.1. [Q9P1Q0-4]
DR RefSeq; NP_057600.2; NM_016516.2. [Q9P1Q0-1]
DR AlphaFoldDB; Q9P1Q0; -.
DR SMR; Q9P1Q0; -.
DR BioGRID; 119600; 38.
DR ComplexPortal; CPX-6208; GARP tethering complex.
DR CORUM; Q9P1Q0; -.
DR DIP; DIP-61627N; -.
DR IntAct; Q9P1Q0; 26.
DR MINT; Q9P1Q0; -.
DR STRING; 9606.ENSP00000272322; -.
DR iPTMnet; Q9P1Q0; -.
DR PhosphoSitePlus; Q9P1Q0; -.
DR BioMuta; VPS54; -.
DR DMDM; 82583721; -.
DR EPD; Q9P1Q0; -.
DR jPOST; Q9P1Q0; -.
DR MassIVE; Q9P1Q0; -.
DR MaxQB; Q9P1Q0; -.
DR PaxDb; Q9P1Q0; -.
DR PeptideAtlas; Q9P1Q0; -.
DR PRIDE; Q9P1Q0; -.
DR ProteomicsDB; 83656; -. [Q9P1Q0-1]
DR ProteomicsDB; 83657; -. [Q9P1Q0-2]
DR ProteomicsDB; 83658; -. [Q9P1Q0-3]
DR ProteomicsDB; 83659; -. [Q9P1Q0-4]
DR ProteomicsDB; 83660; -. [Q9P1Q0-5]
DR Antibodypedia; 30808; 154 antibodies from 26 providers.
DR DNASU; 51542; -.
DR Ensembl; ENST00000272322.9; ENSP00000272322.4; ENSG00000143952.20. [Q9P1Q0-1]
DR Ensembl; ENST00000354504.7; ENSP00000346499.3; ENSG00000143952.20. [Q9P1Q0-3]
DR Ensembl; ENST00000409558.8; ENSP00000386980.3; ENSG00000143952.20. [Q9P1Q0-4]
DR GeneID; 51542; -.
DR KEGG; hsa:51542; -.
DR MANE-Select; ENST00000272322.9; ENSP00000272322.4; NM_016516.3; NP_057600.2.
DR UCSC; uc002scp.4; human. [Q9P1Q0-1]
DR CTD; 51542; -.
DR DisGeNET; 51542; -.
DR GeneCards; VPS54; -.
DR HGNC; HGNC:18652; VPS54.
DR HPA; ENSG00000143952; Low tissue specificity.
DR MIM; 614633; gene.
DR neXtProt; NX_Q9P1Q0; -.
DR OpenTargets; ENSG00000143952; -.
DR PharmGKB; PA134920394; -.
DR VEuPathDB; HostDB:ENSG00000143952; -.
DR eggNOG; KOG2115; Eukaryota.
DR GeneTree; ENSGT00390000000583; -.
DR HOGENOM; CLU_005185_1_0_1; -.
DR InParanoid; Q9P1Q0; -.
DR OMA; SQKQAVM; -.
DR OrthoDB; 449680at2759; -.
DR PhylomeDB; Q9P1Q0; -.
DR TreeFam; TF313700; -.
DR PathwayCommons; Q9P1Q0; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q9P1Q0; -.
DR BioGRID-ORCS; 51542; 242 hits in 1099 CRISPR screens.
DR ChiTaRS; VPS54; human.
DR GenomeRNAi; 51542; -.
DR Pharos; Q9P1Q0; Tbio.
DR PRO; PR:Q9P1Q0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9P1Q0; protein.
DR Bgee; ENSG00000143952; Expressed in sperm and 193 other tissues.
DR ExpressionAtlas; Q9P1Q0; baseline and differential.
DR Genevisible; Q9P1Q0; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0000938; C:GARP complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007041; P:lysosomal transport; IMP:MGI.
DR GO; GO:0050881; P:musculoskeletal movement; IEA:Ensembl.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:MGI.
DR GO; GO:0048515; P:spermatid differentiation; IEA:Ensembl.
DR InterPro; IPR039745; Vps54.
DR InterPro; IPR012501; Vps54_C.
DR InterPro; IPR019515; VPS54_N.
DR PANTHER; PTHR12965; PTHR12965; 1.
DR Pfam; PF07928; Vps54; 1.
DR Pfam; PF10475; Vps54_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..977
FT /note="Vacuolar protein sorting-associated protein 54"
FT /id="PRO_0000148731"
FT REGION 535..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 240..260
FT /evidence="ECO:0000255"
FT COILED 480..507
FT /evidence="ECO:0000255"
FT COILED 582..603
FT /evidence="ECO:0000255"
FT COMPBIAS 535..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..838
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013751"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013752"
FT VAR_SEQ 46..57
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013753"
FT VAR_SEQ 118..126
FT /note="TVYQQEISQ -> MLPTKNRIK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013754"
FT VAR_SEQ 380..415
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013755"
FT VAR_SEQ 964..977
FT /note="DLDLNMAEIWEQKR -> IWT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013756"
FT VARIANT 561
FT /note="S -> C (in dbSNP:rs34015596)"
FT /id="VAR_052944"
FT VARIANT 912
FT /note="M -> I (in dbSNP:rs11558741)"
FT /id="VAR_061983"
FT CONFLICT 130
FT /note="I -> V (in Ref. 1; AAF37319)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="E -> K (in Ref. 1; AAF37319)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="E -> G (in Ref. 1; AAF37319)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="E -> G (in Ref. 1; AAF37319)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="E -> A (in Ref. 1; AAF37319)"
FT /evidence="ECO:0000305"
FT CONFLICT 677..679
FT /note="EER -> VGG (in Ref. 1; AAF37319)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="K -> E (in Ref. 5; BAA92134)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="D -> G (in Ref. 4; AAH41868)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="L -> H (in Ref. 4; AAH41868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 110589 MW; 3290160E3460C836 CRC64;
MASSHSSSPV PQGSSSDVFF KIEVDPSKHI RPVPSLPDVC PKEPTGDSHS LYVAPSLVTD
QHRWTVYHSK VNLPAALNDP RLAKRESDFF TKTWGLDFVD TEVIPSFYLP QISKEHFTVY
QQEISQREKI HERCKNICPP KDTFERTLLH THDKSRTDLE QVPKIFMKPD FALDDSLTFN
SVLPWSHFNT AGGKGNRDAA SSKLLQEKLS HYLDIVEVNI AHQISLRSEA FFHAMTSQHE
LQDYLRKTSQ AVKMLRDKIA QIDKVMCEGS LHILRLALTR NNCVKVYNKL KLMATVHQTQ
PTVQVLLSTS EFVGALDLIA TTQEVLQQEL QGIHSFRHLG SQLCELEKLI DKMMIAEFST
YSHSDLNRPL EDDCQVLEEE RLISLVFGLL KQRKLNFLEI YGEKMVITAK NIIKQCVINK
VSQTEEIDTD VVVKLADQMR MLNFPQWFDL LKDIFSKFTI FLQRVKATLN IIHSVVLSVL
DKNQRTRELE EISQQKNAAK DNSLDTEVAY LIHEGMFISD AFGEGELTPI AVDTTSQRNA
SPNSEPCSSD SVSEPECTTD SSSSKEHTSS SAIPGGVDIM VSEDMKLTDS ELGKLANNIQ
ELLYSASDIC HDRAVKFLMS RAKDGFLEKL NSMEFITLSR LMETFILDTE QICGRKSTSL
LGALQSQAIK FVNRFHEERK TKLSLLLDNE RWKQADVPAE FQDLVDSLSD GKIALPEKKS
GATEERKPAE VLIVEGQQYA VVGTVLLLIR IILEYCQCVD NIPSVTTDML TRLSDLLKYF
NSRSCQLVLG AGALQVVGLK TITTKNLALS SRCLQLIVHY IPVIRAHFEA RLPPKQYSML
RHFDHITKDY HDHIAEISAK LVAIMDSLFD KLLSKYEVKA PVPSACFRNI CKQMTKMHEA
IFDLLPEEQT QMLFLRINAS YKLHLKKQLS HLNVINDGGP QNGLVTADVA FYTGNLQALK
GLKDLDLNMA EIWEQKR
