VPS8_HUMAN
ID VPS8_HUMAN Reviewed; 1428 AA.
AC Q8N3P4; A8K8Q8; B9EIQ1; C9JB61; O94896; Q63HP2; Q9BVP9; Q9H9B0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Vacuolar protein sorting-associated protein 8 homolog;
GN Name=VPS8; Synonyms=KIAA0804;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 608-1428 (ISOFORM 1).
RC TISSUE=Teratocarcinoma, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 100-1428 (ISOFORM 1), AND VARIANTS VAL-83 AND
RP TYR-1165.
RC TISSUE=Amygdala, and Colon endothelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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 218-1428 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-32 AND SER-127, 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 [10]
RP FUNCTION OF THE CORVET COMPLEX, INTERACTION WITH TGFBRAP1, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25266290; DOI=10.1111/tra.12232;
RA Perini E.D., Schaefer R., Stoeter M., Kalaidzidis Y., Zerial M.;
RT "Mammalian CORVET is required for fusion and conversion of distinct early
RT endosome subpopulations.";
RL Traffic 15:1366-1389(2014).
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking of the
CC endocytic membrane transport pathway. Believed to act as a component of
CC the putative CORVET endosomal tethering complexes which is proposed to
CC be involved in the Rab5-to-Rab7 endosome conversion probably
CC implicating MON1A/B, and via binding SNAREs and SNARE complexes to
CC mediate tethering and docking events during SNARE-mediated membrane
CC fusion. The CORVET complex is proposed to function as a Rab5 effector
CC to mediate early endosome fusion probably in specific endosome
CC subpopulations (PubMed:25266290). Functions predominantly in APPL1-
CC containing endosomes (PubMed:25266290). {ECO:0000269|PubMed:25266290,
CC ECO:0000305|PubMed:25266290}.
CC -!- SUBUNIT: Interacts with RAB5C (By similarity). Interacts with TGFBRAP1
CC (PubMed:25266290). Component of the putative class C core
CC vacuole/endosome tethering (CORVET) complex; the core of which composed
CC of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, is
CC associated with VPS8 and TGFBRAP1 (PubMed:25266290).
CC {ECO:0000250|UniProtKB:Q0P5W1, ECO:0000269|PubMed:25266290,
CC ECO:0000305|PubMed:25266290}.
CC -!- INTERACTION:
CC Q8N3P4; Q8WUH2: TGFBRAP1; NbExp=2; IntAct=EBI-7261494, EBI-2954829;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:25266290}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N3P4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N3P4-2; Sequence=VSP_023249, VSP_023250;
CC Name=3;
CC IsoId=Q8N3P4-3; Sequence=VSP_023249;
CC -!- SIMILARITY: Belongs to the VPS8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14322.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH56195.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=CAH56195.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK022945; BAB14322.1; ALT_INIT; mRNA.
DR EMBL; AK292423; BAF85112.1; -; mRNA.
DR EMBL; AL833838; CAD38698.1; -; mRNA.
DR EMBL; BX647915; CAH56195.1; ALT_FRAME; mRNA.
DR EMBL; AC025573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001001; AAH01001.2; -; mRNA.
DR EMBL; BC140768; AAI40769.1; -; mRNA.
DR EMBL; AB018347; BAA34524.1; -; mRNA.
DR CCDS; CCDS46971.1; -. [Q8N3P4-1]
DR CCDS; CCDS46972.1; -. [Q8N3P4-3]
DR RefSeq; NP_001009921.1; NM_001009921.2. [Q8N3P4-1]
DR RefSeq; NP_056118.2; NM_015303.3. [Q8N3P4-3]
DR RefSeq; XP_005247308.1; XM_005247251.3.
DR AlphaFoldDB; Q8N3P4; -.
DR SMR; Q8N3P4; -.
DR BioGRID; 116937; 53.
DR ComplexPortal; CPX-6213; CORVET tethering complex.
DR CORUM; Q8N3P4; -.
DR IntAct; Q8N3P4; 24.
DR MINT; Q8N3P4; -.
DR STRING; 9606.ENSP00000404704; -.
DR iPTMnet; Q8N3P4; -.
DR MetOSite; Q8N3P4; -.
DR PhosphoSitePlus; Q8N3P4; -.
DR BioMuta; VPS8; -.
DR DMDM; 296452997; -.
DR EPD; Q8N3P4; -.
DR jPOST; Q8N3P4; -.
DR MassIVE; Q8N3P4; -.
DR MaxQB; Q8N3P4; -.
DR PaxDb; Q8N3P4; -.
DR PeptideAtlas; Q8N3P4; -.
DR PRIDE; Q8N3P4; -.
DR ProteomicsDB; 71820; -. [Q8N3P4-1]
DR ProteomicsDB; 71821; -. [Q8N3P4-2]
DR ProteomicsDB; 71822; -. [Q8N3P4-3]
DR Antibodypedia; 33827; 79 antibodies from 21 providers.
DR DNASU; 23355; -.
DR Ensembl; ENST00000436792.6; ENSP00000404704.2; ENSG00000156931.16. [Q8N3P4-3]
DR Ensembl; ENST00000446204.6; ENSP00000405483.2; ENSG00000156931.16. [Q8N3P4-2]
DR Ensembl; ENST00000625842.3; ENSP00000487164.1; ENSG00000156931.16. [Q8N3P4-1]
DR GeneID; 23355; -.
DR KEGG; hsa:23355; -.
DR MANE-Select; ENST00000625842.3; ENSP00000487164.1; NM_001009921.3; NP_001009921.1.
DR UCSC; uc003fpb.2; human. [Q8N3P4-1]
DR CTD; 23355; -.
DR DisGeNET; 23355; -.
DR GeneCards; VPS8; -.
DR HGNC; HGNC:29122; VPS8.
DR HPA; ENSG00000156931; Low tissue specificity.
DR MIM; 618366; gene.
DR neXtProt; NX_Q8N3P4; -.
DR OpenTargets; ENSG00000156931; -.
DR PharmGKB; PA142671617; -.
DR PharmGKB; PA142671888; -.
DR VEuPathDB; HostDB:ENSG00000156931; -.
DR eggNOG; KOG2079; Eukaryota.
DR GeneTree; ENSGT00390000010672; -.
DR HOGENOM; CLU_000917_1_2_1; -.
DR InParanoid; Q8N3P4; -.
DR OMA; WAHQDKH; -.
DR OrthoDB; 22166at2759; -.
DR PhylomeDB; Q8N3P4; -.
DR TreeFam; TF314244; -.
DR PathwayCommons; Q8N3P4; -.
DR SignaLink; Q8N3P4; -.
DR BioGRID-ORCS; 23355; 40 hits in 1127 CRISPR screens.
DR ChiTaRS; VPS8; human.
DR GenomeRNAi; 23355; -.
DR Pharos; Q8N3P4; Tbio.
DR PRO; PR:Q8N3P4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8N3P4; protein.
DR Bgee; ENSG00000156931; Expressed in adrenal tissue and 197 other tissues.
DR ExpressionAtlas; Q8N3P4; baseline and differential.
DR Genevisible; Q8N3P4; HS.
DR GO; GO:0033263; C:CORVET complex; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034058; P:endosomal vesicle fusion; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR025941; Vps8_central_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12816; Vps8; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; WD repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..1428
FT /note="Vacuolar protein sorting-associated protein 8
FT homolog"
FT /id="PRO_0000278267"
FT REPEAT 195..236
FT /note="WD"
FT ZN_FING 1258..1310
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1330..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 179..180
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_023249"
FT VAR_SEQ 578..667
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023250"
FT VARIANT 83
FT /note="I -> V (in dbSNP:rs9830734)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_030730"
FT VARIANT 1165
FT /note="H -> Y (in dbSNP:rs11555405)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_030731"
FT VARIANT 1364
FT /note="I -> T (in dbSNP:rs3821750)"
FT /id="VAR_030732"
FT VARIANT 1372
FT /note="R -> H (in dbSNP:rs16859527)"
FT /id="VAR_030733"
FT CONFLICT 433
FT /note="E -> G (in Ref. 2; CAH56195)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="K -> N (in Ref. 2; CAH56195)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="A -> S (in Ref. 1; BAB14322)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="Missing (in Ref. 2; CAH56195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042
FT /note="T -> A (in Ref. 1; BAB14322)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="Q -> L (in Ref. 2; CAH56195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="E -> G (in Ref. 1; BAB14322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1428 AA; 161754 MW; 97FB5E8D453BBCB6 CRC64;
MENEPDHENV EQSLCAKTSE EELNKSFNLE ASLSKFSYID MDKELEFKND LIDDKEFDIP
QVDTPPTLES ILNETDDEDE SFILEDPTLL NIDTIDSHSY DTSSVASSDS GDRTNLKRKK
KLPDSFSLHG SVMRHSLLKG ISAQIVSAAD KVDAGLPTAI AVSSLIAVGT SHGLALIFGK
DQNQALRLCL GSTSVGGQYG AISALSINND CSRLLCGFAK GQITMWDLAS GKLLRSITDA
HPPGTAILHI KFTDDPTLAI CNDSGGSVFE LTFKRVMGVR TCESRCLFSG SKGEVCCIEP
LHSKPELKDH PITQFSLLAM ASLTKILVIG LKPSLKVWMT FPYGRMDPSS VPLLAWHFVA
VQNYVNPMLA FCRGDVVHFL LVKRDESGAI HVTKQKHLHL YYDLINFTWI NSRTVVLLDS
VEKLHVIDRQ TQEELETVEI SEVQLVYNSS HFKSLATGGN VSQALALVGE KACYQSISSY
GGQIFYLGTK SVYVMMLRSW RERVDHLLKQ DCLTEALALA WSFHEGKAKA VVGLSGDASK
RKAIVADRMV EILFHYADRA LKKCPDQGKI QVMEQHFQDM VPVIVDYCLL LQRKDLLFSQ
MYDKLSENSV AKGVFLECLE PYILSDKLVG ITPQVMKDLI VHFQDKKLME NVEALIVHMD
ITSLDIQQVV LMCWENRLYD AMIYVYNRGM NEFISPMEKL FRVIAPPLNA GKTLTDEQVV
MGNKLLVYIS CCLAGRAYPL GDIPEDLVPL VKNQVFEFLI RLHSAEASPE EEIYPYIRTL
LHFDTREFLN VLALTFEDFK NDKQAVEYQQ RIVDILLKVM VENSDFTPSQ VGCLFTFLAR
QLAKPDNTLF VNRTLFDQVL EFLCSPDDDS RHSERQQVLL ELLQAGGIVQ FEESRLIRMA
EKAEFYQICE FMYEREHQYD KIIDCYLRDP LREEEVFNYI HNILSIPGHS AEEKQSVWQK
AMDHIEELVS LKPCKAAELV ATHFSGHIET VIKKLQNQVL LFKFLRSLLD PREGIHVNQE
LLQISPCITE QFIELLCQFN PTQVIETLQV LECYRLEETI QITQKYQLHE VTAYLLEKKG
DIHGAFLIML ERLQSKLQEV THQGENTKED PSLKDVEDTM VETIALCQRN SHNLNQQQRE
ALWFPLLEAM MAPQKLSSSA IPHLHSEALK SLTMQVLNSM AAFIALPSIL QRILQDPVYG
KGKLGEIQGL ILGMLDTFNY EQTLLETTTS LLNQDLHWSL CNLRASVTRG LNPKQDYCSI
CLQQYKRRQE MADEIIVFSC GHLYHSFCLQ NKECTVEFEG QTRWTCYKCS SSNKVGKLSE
NSSEIKKGRI TPSQVKMSPS YHQSKGDPTA KKGTSEPVLD PQQIQAFDQL CRLYRGSSRL
ALLTELSQNR SSESYRPFSG SQSAPAFNSI FQNENFQLQL IPPPVTED
