SC16B_HUMAN
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 03-AUG-2022, entry version 133.
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}.
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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; 7.
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; Q96JE7; -.
DR PeptideAtlas; Q96JE7; -.
DR PRIDE; 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; 126 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 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; 235062at2759; -.
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 1060 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 92 other tissues.
DR ExpressionAtlas; Q96JE7; baseline and differential.
DR Genevisible; Q96JE7; HS.
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 InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
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
