ID SEC63_HUMAN Reviewed; 760 AA. AC Q9UGP8; O95380; Q5THN4; Q86VS9; Q8IWL0; Q9NTE0; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 198. DE RecName: Full=Translocation protein SEC63 homolog; GN Name=SEC63 {ECO:0000303|PubMed:28375157, ECO:0000312|HGNC:HGNC:21082}; GN Synonyms=SEC63L; 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]. RX PubMed=10543453; DOI=10.1515/bc.1999.142; RA Skowronek M.H., Rotter M., Haas I.G.; RT "Molecular characterization of a novel mammalian DnaJ-like Sec63p RT homolog."; RL Biol. Chem. 380:1133-1138(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10799540; DOI=10.1074/jbc.275.19.14550; RA Meyer H.-A., Grau H., Kraft R., Kostka S., Prehn S., Kalies K.-U., RA Hartmann E.; RT "Mammalian Sec61 is associated with Sec62 and Sec63."; RL J. Biol. Chem. 275:14550-14557(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-556. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Kidney, and Leukocyte; 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 129-760. 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 [6] RP TISSUE SPECIFICITY, AND VARIANT PCLD2 GLU-568 DEL. RX PubMed=15133510; DOI=10.1038/ng1357; RA Davila S., Furu L., Gharavi A.G., Tian X., Onoe T., Qian Q., Li A., Cai Y., RA Kamath P.S., King B.F., Azurmendi P.J., Tahvanainen P., Kaeaeriaeinen H., RA Hoeckerstedt K., Devuyst O., Pirson Y., Martin R.S., Lifton R.P., RA Tahvanainen E., Torres V.E., Somlo S.; RT "Mutations in SEC63 cause autosomal dominant polycystic liver disease."; RL Nat. Genet. 36:575-577(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742 AND SER-748, AND RP IDENTIFICATION BY 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 [8] 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 [9] RP FUNCTION. RX PubMed=22375059; DOI=10.1242/jcs.096727; RA Lang S., Benedix J., Fedeles S.V., Schorr S., Schirra C., Schaeuble N., RA Jalal C., Greiner M., Hassdenteufel S., Tatzelt J., Kreutzer B., RA Edelmann L., Krause E., Rettig J., Somlo S., Zimmermann R., Dudek J.; RT "Different effects of Sec61alpha, Sec62 and Sec63 depletion on transport of RT polypeptides into the endoplasmic reticulum of mammalian cells."; RL J. Cell Sci. 125:1958-1969(2012). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-537, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] 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 [12] RP FUNCTION, AND MUTAGENESIS OF HIS-132 AND 735-GLY--ASP-760. RX PubMed=29719251; DOI=10.1016/j.celrep.2018.03.122; RA Hassdenteufel S., Johnson N., Paton A.W., Paton J.C., High S., RA Zimmermann R.; RT "Chaperone-Mediated Sec61 Channel Gating during ER Import of Small RT Precursor Proteins Overcomes Sec61 Inhibitor-Reinforced Energy Barrier."; RL Cell Rep. 23:1373-1386(2018). RN [13] RP INVOLVEMENT IN PCLD2, AND VARIANTS PCLD2 7-GLN--ASP-760 DEL; RP 58-TRP--ASP-760 DEL; 98-ARG--ASP-760 DEL; 233-TYR--ASP-760 DEL; RP 239-ARG--ASP-760 DEL; 297-TYR--ASP-760 DEL; 417-GLU--ASP-760 DEL; RP 550-LYS--ASP-760 DEL AND 601-GLN--ASP-760 DEL. RX PubMed=28375157; DOI=10.1172/jci90129; RA Besse W., Dong K., Choi J., Punia S., Fedeles S.V., Choi M., RA Gallagher A.R., Huang E.B., Gulati A., Knight J., Mane S., Tahvanainen E., RA Tahvanainen P., Sanna-Cherchi S., Lifton R.P., Watnick T., Pei Y.P., RA Torres V.E., Somlo S.; RT "Isolated polycystic liver disease genes define effectors of polycystin-1 RT function."; RL J. Clin. Invest. 127:1772-1785(2017). CC -!- FUNCTION: Mediates cotranslational and post-translational transport of CC certain precursor polypeptides across endoplasmic reticulum (ER) CC (PubMed:22375059, PubMed:29719251). Proposed to play an auxiliary role CC in recognition of precursors with short and apolar signal peptides. May CC cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small CC presecretory proteins into the SEC61 channel-forming translocon CC complex, triggering channel opening for polypeptide translocation to CC the ER lumen (PubMed:29719251). Required for efficient PKD1/Polycystin- CC 1 biogenesis and trafficking to the plasma membrane of the primary CC cilia (By similarity). {ECO:0000250|UniProtKB:Q8VHE0, CC ECO:0000269|PubMed:22375059, ECO:0000269|PubMed:29719251}. CC -!- SUBUNIT: The ER translocon complex consists of channel-forming core CC components SEC61A1, SEC61B and SEC61G and different auxiliary CC components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P82008}. CC -!- INTERACTION: CC Q9UGP8; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1045560, EBI-16439278; CC Q9UGP8; P97346: Nxn; Xeno; NbExp=6; IntAct=EBI-1045560, EBI-309684; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in the liver. CC {ECO:0000269|PubMed:15133510}. CC -!- DISEASE: Polycystic liver disease 2 with or without kidney cysts CC (PCLD2) [MIM:617004]: An autosomal dominant hepatobiliary disease CC characterized by overgrowth of biliary epithelium and supportive CC connective tissue, resulting in multiple liver cysts. A subset of CC patients may develop kidney cysts that usually do not result in CC clinically significant renal disease. {ECO:0000269|PubMed:15133510, CC ECO:0000269|PubMed:28375157}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH23598.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={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; AJ011779; CAB46275.1; -; mRNA. DR EMBL; AF100141; AAC83375.1; -; mRNA. DR EMBL; AL024507; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC023598; AAH23598.1; ALT_SEQ; mRNA. DR EMBL; BC047221; AAH47221.1; -; mRNA. DR EMBL; BC048287; AAH48287.1; -; mRNA. DR EMBL; AL137338; CAB70701.1; -; mRNA. DR CCDS; CCDS5061.1; -. DR PIR; T46504; T46504. DR RefSeq; NP_009145.1; NM_007214.4. DR AlphaFoldDB; Q9UGP8; -. DR BioGRID; 116397; 364. DR IntAct; Q9UGP8; 53. DR MINT; Q9UGP8; -. DR STRING; 9606.ENSP00000357998; -. DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family. DR CarbonylDB; Q9UGP8; -. DR GlyGen; Q9UGP8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UGP8; -. DR PhosphoSitePlus; Q9UGP8; -. DR SwissPalm; Q9UGP8; -. DR BioMuta; SEC63; -. DR DMDM; 18203500; -. DR EPD; Q9UGP8; -. DR jPOST; Q9UGP8; -. DR MassIVE; Q9UGP8; -. DR MaxQB; Q9UGP8; -. DR PaxDb; 9606-ENSP00000357998; -. DR PeptideAtlas; Q9UGP8; -. DR ProteomicsDB; 84254; -. DR Pumba; Q9UGP8; -. DR Antibodypedia; 32190; 160 antibodies from 24 providers. DR DNASU; 11231; -. DR Ensembl; ENST00000369002.9; ENSP00000357998.4; ENSG00000025796.14. DR GeneID; 11231; -. DR KEGG; hsa:11231; -. DR MANE-Select; ENST00000369002.9; ENSP00000357998.4; NM_007214.5; NP_009145.1. DR UCSC; uc003psc.5; human. DR AGR; HGNC:21082; -. DR CTD; 11231; -. DR DisGeNET; 11231; -. DR GeneCards; SEC63; -. DR HGNC; HGNC:21082; SEC63. DR HPA; ENSG00000025796; Low tissue specificity. DR MalaCards; SEC63; -. DR MIM; 608648; gene. DR MIM; 617004; phenotype. DR neXtProt; NX_Q9UGP8; -. DR OpenTargets; ENSG00000025796; -. DR Orphanet; 2924; Isolated polycystic liver disease. DR PharmGKB; PA134936990; -. DR VEuPathDB; HostDB:ENSG00000025796; -. DR eggNOG; KOG0721; Eukaryota. DR GeneTree; ENSGT00390000001965; -. DR HOGENOM; CLU_014210_1_0_1; -. DR InParanoid; Q9UGP8; -. DR OMA; RAILHAH; -. DR OrthoDB; 1605at2759; -. DR PhylomeDB; Q9UGP8; -. DR TreeFam; TF105904; -. DR PathwayCommons; Q9UGP8; -. DR SignaLink; Q9UGP8; -. DR SIGNOR; Q9UGP8; -. DR BioGRID-ORCS; 11231; 433 hits in 1158 CRISPR screens. DR ChiTaRS; SEC63; human. DR GeneWiki; SEC63; -. DR GenomeRNAi; 11231; -. DR Pharos; Q9UGP8; Tbio. DR PRO; PR:Q9UGP8; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9UGP8; Protein. DR Bgee; ENSG00000025796; Expressed in colonic epithelium and 217 other cell types or tissues. DR ExpressionAtlas; Q9UGP8; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0031207; C:Sec62/Sec63 complex; IBA:GO_Central. DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:Ensembl. DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:MGI. DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IMP:UniProtKB. DR GO; GO:0006612; P:protein targeting to membrane; TAS:ProtInc. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:MGI. DR CDD; cd06257; DnaJ; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR036869; J_dom_sf. DR InterPro; IPR004179; Sec63-dom. DR PANTHER; PTHR24075; SEC63 DOMAIN-CONTAINING; 1. DR PANTHER; PTHR24075:SF0; TRANSLOCATION PROTEIN SEC63 HOMOLOG; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF02889; Sec63; 2. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SMART; SM00973; Sec63; 1. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR Genevisible; Q9UGP8; HS. PE 1: Evidence at protein level; KW Chaperone; Coiled coil; Disease variant; Endoplasmic reticulum; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..760 FT /note="Translocation protein SEC63 homolog" FT /id="PRO_0000071097" FT TOPO_DOM 1..14 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 15..35 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 36..69 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 70..90 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 91..188 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 210..760 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 104..165 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT DOMAIN 197..541 FT /note="SEC63 1" FT DOMAIN 637..714 FT /note="SEC63 2" FT REGION 492..617 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 720..760 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 597..635 FT /evidence="ECO:0000255" FT COMPBIAS 520..535 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 540..554 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 576..617 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 734..760 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 537 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 742 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 748 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VARIANT 7..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080944" FT VARIANT 58..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080945" FT VARIANT 98..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080946" FT VARIANT 233..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080947" FT VARIANT 239..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080948" FT VARIANT 297..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080949" FT VARIANT 417..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080950" FT VARIANT 550..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080951" FT VARIANT 556 FT /note="V -> I (in dbSNP:rs17854547)" FT /evidence="ECO:0000269|PubMed:14574404" FT /id="VAR_061146" FT VARIANT 568 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:15133510" FT /id="VAR_019645" FT VARIANT 601..760 FT /note="Missing (in PCLD2)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080952" FT MUTAGEN 132 FT /note="H->Q: Reduces cotranslational translocation of APLN FT precursor/preproapelin." FT /evidence="ECO:0000269|PubMed:29719251" FT MUTAGEN 735..760 FT /note="Missing: Reduces cotranslational translocation of FT APLN precursor/preproapelin." FT /evidence="ECO:0000269|PubMed:29719251" FT CONFLICT 115 FT /note="A -> V (in Ref. 4; AAH23598)" FT /evidence="ECO:0000305" SQ SEQUENCE 760 AA; 87997 MW; 81BBF269A3FCCF0D CRC64; MAGQQFQYDD SGNTFFYFLT SFVGLIVIPA TYYLWPRDQN AEQIRLKNIR KVYGRCMWYR LRLLKPQPNI IPTVKKIVLL AGWALFLFLA YKVSKTDREY QEYNPYEVLN LDPGATVAEI KKQYRLLSLK YHPDKGGDEV MFMRIAKAYA ALTDEESRKN WEEFGNPDGP QATSFGIALP AWIVDQKNSI LVLLVYGLAF MVILPVVVGS WWYRSIRYSG DQILIRTTQI YTYFVYKTRN MDMKRLIMVL AGASEFDPQY NKDATSRPTD NILIPQLIRE IGSINLKKNE PPLTCPYSLK ARVLLLSHLA RMKIPETLEE DQQFMLKKCP ALLQEMVNVI CQLIVMARNR EEREFRAPTL ASLENCMKLS QMAVQGLQQF KSPLLQLPHI EEDNLRRVSN HKKYKIKTIQ DLVSLKESDR HTLLHFLEDE KYEEVMAVLG SFPYVTMDIK SQVLDDEDSN NITVGSLVTV LVKLTRQTMA EVFEKEQSIC AAEEQPAEDG QGETNKNRTK GGWQQKSKGP KKTAKSKKKK PLKKKPTPVL LPQSKQQKQK QANGVVGNEA AVKEDEEEVS DKGSDSEEEE TNRDSQSEKD DGSDRDSDRE QDEKQNKDDE AEWQELQQSI QRKERALLET KSKITHPVYS LYFPEEKQEW WWLYIADRKE QTLISMPYHV CTLKDTEEVE LKFPAPGKPG NYQYTVFLRS DSYMGLDQIK PLKLEVHEAK PVPENHPQWD TAIEGDEDQE DSEGFEDSFE EEEEEEEDDD //