ID SC16B_HUMAN Reviewed; 1060 AA. AC Q96JE7; A3EYF1; Q5HYF6; Q8N7D6; Q96GX6; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 2. DT 24-JAN-2024, entry version 140. DE RecName: Full=Protein transport protein Sec16B; DE AltName: Full=Leucine zipper transcription regulator 2; DE AltName: Full=Regucalcin gene promoter region-related protein p117; DE Short=RGPR-p117; DE AltName: Full=SEC16 homolog B; GN Name=SEC16B; Synonyms=KIAA1928, LZTR2, RGPR, SEC16S; 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), AND VARIANT ARG-730. RC TISSUE=Liver; RX PubMed=11605020; DOI=10.3892/ijmm.8.5.513; RA Misawa H., Yamaguchi M.; RT "Molecular cloning and sequencing of the cDNA coding for a novel regucalcin RT gene promoter region-related protein in rat, mouse and human liver."; RL Int. J. Mol. Med. 8:513-520(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-292, FUNCTION, SUBUNIT, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=17192411; DOI=10.1091/mbc.e06-08-0707; RA Bhattacharyya D., Glick B.S.; RT "Two mammalian Sec16 homologues have nonredundant functions in endoplasmic RT reticulum (ER) export and transitional ER organization."; RL Mol. Biol. Cell 18:839-849(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-845; RP ALA-864 AND ASN-873. RC TISSUE=Retina; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-292. RC TISSUE=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 [6] RP TISSUE SPECIFICITY. RX PubMed=12244571; DOI=10.1002/jcb.10289; RA Misawa H., Yamaguchi M.; RT "Gene expression for a novel protein RGPR-p117 in various species: the RT stimulation by intracellular signaling factors."; RL J. Cell. Biochem. 87:188-193(2002). RN [7] RP INTERACTION WITH TFG, AND SUBCELLULAR LOCATION. RX PubMed=21478858; DOI=10.1038/ncb2225; RA Witte K., Schuh A.L., Hegermann J., Sarkeshik A., Mayers J.R., Schwarze K., RA Yates J.R. III, Eimer S., Audhya A.; RT "TFG-1 function in protein secretion and oncogenesis."; RL Nat. Cell Biol. 13:550-558(2011). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21768384; DOI=10.1073/pnas.1103283108; RA Yonekawa S., Furuno A., Baba T., Fujiki Y., Ogasawara Y., Yamamoto A., RA Tagaya M., Tani K.; RT "Sec16B is involved in the endoplasmic reticulum export of the peroxisomal RT membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12746-12751(2011). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC16A AND SEC13. RX PubMed=22355596; DOI=10.1038/srep00077; RA Budnik A., Heesom K.J., Stephens D.J.; RT "Characterization of human Sec16B: indications of specialized, non- RT redundant functions."; RL Sci. Rep. 1:77-77(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-167; SER-254; SER-258 RP AND THR-858, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). CC -!- FUNCTION: Plays a role in the organization of the endoplasmic reticulum CC exit sites (ERES), also known as transitional endoplasmic reticulum CC (tER). Required for secretory cargo traffic from the endoplasmic CC reticulum to the Golgi apparatus (PubMed:17192411, PubMed:21768384, CC PubMed:22355596). Involved in peroxisome biogenesis. Regulates the CC transport of peroxisomal biogenesis factors PEX3 and PEX16 from the ER CC to peroxisomes (PubMed:21768384). {ECO:0000269|PubMed:17192411, CC ECO:0000269|PubMed:21768384, ECO:0000303|PubMed:22355596}. CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a CC heteromeric complex (PubMed:17192411, PubMed:22355596). Interacts with CC TFG (PubMed:21478858). Interacts with SEC13 (PubMed:22355596). CC {ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:21478858, CC ECO:0000269|PubMed:22355596}. CC -!- INTERACTION: CC Q96JE7-2; P55735: SEC13; NbExp=6; IntAct=EBI-10215083, EBI-1046596; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:21768384}; Peripheral membrane protein CC {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. Note=Localizes to endoplasmic reticulum CC exit sites (ERES), also known as transitional endoplasmic reticulum CC (tER). {ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:21478858, CC ECO:0000269|PubMed:21768384, ECO:0000269|PubMed:22355596}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96JE7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96JE7-2; Sequence=VSP_034373, VSP_034374; CC Name=3; CC IsoId=Q96JE7-3; Sequence=VSP_034371, VSP_034372, VSP_034375, CC VSP_034376; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12244571, CC ECO:0000269|PubMed:17192411}. CC -!- SIMILARITY: Belongs to the SEC16 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; AB063357; BAB61035.1; -; mRNA. DR EMBL; EF125213; ABN42197.1; -; mRNA. DR EMBL; AK098627; BAC05357.1; -; mRNA. DR EMBL; BX647819; CAI46016.1; -; mRNA. DR EMBL; BC009106; AAH09106.1; -; mRNA. DR CCDS; CCDS44281.1; -. [Q96JE7-1] DR RefSeq; NP_149118.2; NM_033127.2. [Q96JE7-1] DR AlphaFoldDB; Q96JE7; -. DR SMR; Q96JE7; -. DR BioGRID; 124624; 9. DR IntAct; Q96JE7; 3. DR STRING; 9606.ENSP00000308339; -. DR iPTMnet; Q96JE7; -. DR PhosphoSitePlus; Q96JE7; -. DR BioMuta; SEC16B; -. DR DMDM; 193806482; -. DR MassIVE; Q96JE7; -. DR PaxDb; 9606-ENSP00000308339; -. DR PeptideAtlas; Q96JE7; -. DR ProteomicsDB; 76948; -. [Q96JE7-1] DR ProteomicsDB; 76949; -. [Q96JE7-2] DR ProteomicsDB; 76950; -. [Q96JE7-3] DR TopDownProteomics; Q96JE7-1; -. [Q96JE7-1] DR Antibodypedia; 35113; 143 antibodies from 28 providers. DR DNASU; 89866; -. DR Ensembl; ENST00000308284.11; ENSP00000308339.6; ENSG00000120341.19. [Q96JE7-1] DR GeneID; 89866; -. DR KEGG; hsa:89866; -. DR MANE-Select; ENST00000308284.11; ENSP00000308339.6; NM_033127.4; NP_149118.2. DR UCSC; uc001gli.2; human. [Q96JE7-1] DR AGR; HGNC:30301; -. DR AGR; HGNC:53757; -. DR CTD; 89866; -. DR DisGeNET; 89866; -. DR GeneCards; SEC16B; -. DR HGNC; HGNC:30301; SEC16B. DR HPA; ENSG00000120341; Tissue enhanced (intestine, liver). DR MIM; 612855; gene. DR neXtProt; NX_Q96JE7; -. DR OpenTargets; ENSG00000120341; -. DR PharmGKB; PA162402680; -. DR VEuPathDB; HostDB:ENSG00000120341; -. DR eggNOG; KOG1913; Eukaryota. DR GeneTree; ENSGT00940000160138; -. DR HOGENOM; CLU_010575_0_0_1; -. DR InParanoid; Q96JE7; -. DR OMA; HPRDEGH; -. DR OrthoDB; 1361743at2759; -. DR PhylomeDB; Q96JE7; -. DR PathwayCommons; Q96JE7; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR SignaLink; Q96JE7; -. DR SIGNOR; Q96JE7; -. DR BioGRID-ORCS; 89866; 6 hits in 1138 CRISPR screens. DR GeneWiki; SEC16B; -. DR GenomeRNAi; 89866; -. DR Pharos; Q96JE7; Tbio. DR PRO; PR:Q96JE7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96JE7; Protein. DR Bgee; ENSG00000120341; Expressed in right lobe of liver and 93 other cell types or tissues. DR ExpressionAtlas; Q96JE7; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:InterPro. DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro. DR GO; GO:0007029; P:endoplasmic reticulum organization; IDA:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB. DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central. DR GO; GO:0016559; P:peroxisome fission; IMP:UniProtKB. DR GO; GO:0007031; P:peroxisome organization; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IMP:UniProtKB. DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR CDD; cd09233; ACE1-Sec16-like; 1. DR Gene3D; 1.25.40.1030; -; 1. DR InterPro; IPR024298; ACE1_Sec16_Sec31. DR InterPro; IPR024880; Sec16. DR InterPro; IPR024340; Sec16_CCD. DR PANTHER; PTHR13402:SF11; PROTEIN TRANSPORT PROTEIN SEC16B; 1. DR PANTHER; PTHR13402; RGPR-RELATED; 1. DR Pfam; PF12932; Sec16; 1. DR Pfam; PF12931; Sec16_C; 1. DR Genevisible; Q96JE7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; ER-Golgi transport; KW Golgi apparatus; Membrane; Peroxisome biogenesis; Phosphoprotein; KW Protein transport; Reference proteome; Transport. FT CHAIN 1..1060 FT /note="Protein transport protein Sec16B" FT /id="PRO_0000341974" FT REGION 1..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 34..224 FT /note="Required for endoplasmic reticulum localization" FT REGION 163..236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 245..264 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 271..713 FT /note="Central conserved domain (CCD); required for FT localization to endoplasmic reticulum exit sites" FT /evidence="ECO:0000269|PubMed:21768384" FT REGION 711..733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 770..796 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 834..1060 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 18..48 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 49..67 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 166..195 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..236 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 834..852 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..906 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 913..933 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 941..958 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1033..1060 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q75N33" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XT4" FT MOD_RES 191 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XT4" FT MOD_RES 254 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 858 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 868 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q75N33" FT MOD_RES 871 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XT4" FT MOD_RES 874 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XT4" FT MOD_RES 882 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XT4" FT MOD_RES 883 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XT4" FT VAR_SEQ 1..435 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_034371" FT VAR_SEQ 436..515 FT /note="ETPAQIVEKFTRLLYYGRKKEALEWAMKNHLWGHALFLSSKMDPQTYSWVMS FT GFTSTLALNDPLQTLFQLMSGRIPQAAT -> MRGFVHFHHAAYSFLPPGGILLPLHRP FT SWATWLDFLILKVAVGTRLHRVPVKIKRMCVNGLCRARKHRHL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_034372" FT VAR_SEQ 592..624 FT /note="SQEFLKFATTEAIQRTEIFEYCQMLGRPKSFIP -> RYATWEKGNSKDIFQ FT GTVLALVGFYGSSFHFLM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034373" FT VAR_SEQ 625..1060 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034374" FT VAR_SEQ 942..986 FT /note="ETPRASSPHQAGLGLSLTPSPESPPLPDVSAFSRGRGGGEGRGSA -> VGV FT KAEDPHPAGGQLRALGLEACLDQRVFPLSSAPTLVFFFLHLP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_034375" FT VAR_SEQ 987..1060 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_034376" FT VARIANT 292 FT /note="H -> R (in dbSNP:rs12040910)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17192411" FT /id="VAR_044130" FT VARIANT 730 FT /note="G -> R (in dbSNP:rs943762)" FT /evidence="ECO:0000269|PubMed:11605020" FT /id="VAR_044131" FT VARIANT 845 FT /note="Q -> H (in dbSNP:rs7522194)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_044132" FT VARIANT 864 FT /note="P -> A (in dbSNP:rs591120)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_044133" FT VARIANT 873 FT /note="S -> N (in dbSNP:rs3813649)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_044134" FT CONFLICT 134 FT /note="Q -> R (in Ref. 4; CAI46016)" FT /evidence="ECO:0000305" FT CONFLICT 195 FT /note="Q -> R (in Ref. 2; ABN42197)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="A -> AE (in Ref. 4; CAI46016 and 5; AAH09106)" FT /evidence="ECO:0000305" FT CONFLICT 514 FT /note="A -> T (in Ref. 4; CAI46016)" FT /evidence="ECO:0000305" FT CONFLICT 929 FT /note="A -> S (in Ref. 4; CAI46016)" FT /evidence="ECO:0000305" SQ SEQUENCE 1060 AA; 116604 MW; B1D1483EAB45E676 CRC64; MELWAPQRLP QTRGKATAPS KDPDRGFRRD GHHRPVPHSW HNGERFHQWQ DNRGSPQPQQ EPRADHQQQP HYASRPGDWH QPVSGVDYYE GGYRNQLYSR PGYENSYQSY QSPTMREEYA YGSYYYHGHP QWLQEERVPR QRSPYIWHED YREQKYLDEH HYENQHSPFG TNSETHFQSN SRNPCKDSPA SNSGQEWPGE LFPGSLLAEA QKNKPSLASE SNLLQQRESG LSSSSYELSQ YIRDAPERDD PPASAAWSPV QADVSSAGPK APMKFYIPHV PVSFGPGGQL VHVGPSSPTD GQAALVELHS MEVILNDSEE QEEMRSFSGP LIREDVHKVD IMTFCQQKAA QSCKSETLGS RDSALLWQLL VLLCRQNGSM VGSDIAELLM QDCKKLEKYK RQPPVANLIN LTDEDWPVLS SGTPNLLTGE IPPSVETPAQ IVEKFTRLLY YGRKKEALEW AMKNHLWGHA LFLSSKMDPQ TYSWVMSGFT STLALNDPLQ TLFQLMSGRI PQAATCCGEK QWGDWRPHLA VILSNQAGDP ELYQRAIVAI GDTLAGKGLV EAAHFCYLMA HVPFGHYTVK TDHLVLLGSS HSQEFLKFAT TEAIQRTEIF EYCQMLGRPK SFIPSFQVYK LLYASRLADY GLVSQALHYC EAIGAAVLSQ GESSHPVLLV ELIKLAEKLK LSDPLVLERR SGDRDLEPDW LAQLRRQLEQ KVAGDIGDPH PTRSDISGAG GTTTENTFYQ DFSGCQGYSE APGYRSALWL TPEQTCLLQP SPQQPFPLQP GSYPAGGGAG QTGTPRPFYS VPETHLPGTG SSVAVTEATG GTVWEEMLQT HLGPGENTVS QETSQPPDGQ EVISKPQTPL AARPRSISES SASSAKEDEK ESSDEADKNS PRNTAQRGKL GDGKEHTKSS GFGWFSWFRS KPTKNASPAG DEDSSDSPDS EETPRASSPH QAGLGLSLTP SPESPPLPDV SAFSRGRGGG EGRGSASSGG AAAGAGVGGL SGPESVSFEL CSNPGVLLPP PALKGAVPLY NPSQVPQLPT ATSLNRPNRL AQRRYPTQPC //