PREB_HUMAN
ID PREB_HUMAN Reviewed; 417 AA.
AC Q9HCU5; Q53SZ8; Q9UH94;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Prolactin regulatory element-binding protein;
DE AltName: Full=Mammalian guanine nucleotide exchange factor mSec12;
GN Name=PREB; Synonyms=SEC12;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10920239; DOI=10.1007/s003350010142;
RA Taylor Clelland C.L., Levy B., McKie J.M., Duncan A.M.V., Hirschhorn K.,
RA Bancroft C.;
RT "Cloning and characterization of human PREB; a gene that maps to a genomic
RT region associated with trisomy 2p syndrome.";
RL Mamm. Genome 11:675-681(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Edgar A.J., Polak J.M.;
RT "The human and mouse homologues of rat prolactin regulatory element binding
RT protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12735795; DOI=10.1186/1471-2164-4-18;
RA Edgar A.J.;
RT "The gene structure and expression of human ABHD1: overlapping
RT polyadenylation signal sequence with Sec12.";
RL BMC Genomics 4:18-18(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Uterus;
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 [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 INTERACTION WITH MIA2, AND SUBCELLULAR LOCATION.
RX PubMed=25202031; DOI=10.1083/jcb.201312062;
RA Saito K., Yamashiro K., Shimazu N., Tanabe T., Kontani K., Katada T.;
RT "Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is
RT required for collagen export.";
RL J. Cell Biol. 206:751-762(2014).
RN [10]
RP IDENTIFICATION BY 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 INTERACTION WITH MIA2.
RX PubMed=27170179; DOI=10.1091/mbc.e16-03-0180;
RA Tanabe T., Maeda M., Saito K., Katada T.;
RT "Dual function of cTAGE5 in collagen export from the endoplasmic
RT reticulum.";
RL Mol. Biol. Cell 27:2008-2013(2016).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=28442536; DOI=10.1083/jcb.201703084;
RA Maeda M., Katada T., Saito K.;
RT "TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient
RT secretion.";
RL J. Cell Biol. 216:1731-1743(2017).
CC -!- FUNCTION: Guanine nucleotide exchange factor that specifically
CC activates the small GTPase SAR1B. Mediates the recruitment of SAR1B and
CC other COPII coat components to endoplasmic reticulum membranes and is
CC therefore required for the formation of COPII transport vesicles from
CC the ER. {ECO:0000250|UniProtKB:Q9WTV0, ECO:0000250|UniProtKB:Q9WUQ2}.
CC -!- FUNCTION: Was first identified based on its probable role in the
CC regulation of pituitary gene transcription. Binds to the prolactin gene
CC (PRL) promoter and seems to activate transcription.
CC {ECO:0000250|UniProtKB:Q9WTV0}.
CC -!- SUBUNIT: Interacts with SAR1B (GDP-bound form) (By similarity).
CC Interacts with MIA2; recruits PREB to endoplasmic reticulum exit sites
CC (PubMed:25202031, PubMed:27170179). {ECO:0000250|UniProtKB:Q9WUQ2,
CC ECO:0000269|PubMed:25202031, ECO:0000269|PubMed:27170179}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9WTV0}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9WTV0}. Nucleus {ECO:0000250|UniProtKB:Q9WTV0}.
CC Note=Concentrates at endoplasmic reticulum exit sites (ERES), also
CC known as transitional endoplasmic reticulum (tER).
CC {ECO:0000269|PubMed:25202031, ECO:0000269|PubMed:28442536}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10920239,
CC ECO:0000269|PubMed:12735795}.
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DR EMBL; AF226684; AAG01692.1; -; mRNA.
DR EMBL; AF203687; AAF19192.1; -; mRNA.
DR EMBL; AF227166; AAF74572.1; -; Genomic_DNA.
DR EMBL; AK023064; BAB14385.1; -; mRNA.
DR EMBL; AC013403; AAX93170.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00627.1; -; Genomic_DNA.
DR EMBL; BC002765; AAH02765.1; -; mRNA.
DR EMBL; BC012890; AAH12890.1; -; mRNA.
DR EMBL; BC016472; AAH16472.1; -; mRNA.
DR EMBL; BC041032; AAH41032.1; -; mRNA.
DR CCDS; CCDS1738.1; -.
DR RefSeq; NP_001317414.1; NM_001330485.1.
DR RefSeq; NP_001317415.1; NM_001330486.1.
DR RefSeq; NP_037520.1; NM_013388.5.
DR PDB; 5TF2; X-ray; 2.80 A; A=1-389.
DR PDBsum; 5TF2; -.
DR AlphaFoldDB; Q9HCU5; -.
DR SMR; Q9HCU5; -.
DR BioGRID; 115419; 182.
DR CORUM; Q9HCU5; -.
DR IntAct; Q9HCU5; 32.
DR MINT; Q9HCU5; -.
DR STRING; 9606.ENSP00000260643; -.
DR TCDB; 8.A.92.1.10; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; Q9HCU5; -.
DR PhosphoSitePlus; Q9HCU5; -.
DR SwissPalm; Q9HCU5; -.
DR BioMuta; PREB; -.
DR DMDM; 55977881; -.
DR EPD; Q9HCU5; -.
DR jPOST; Q9HCU5; -.
DR MassIVE; Q9HCU5; -.
DR MaxQB; Q9HCU5; -.
DR PaxDb; Q9HCU5; -.
DR PeptideAtlas; Q9HCU5; -.
DR PRIDE; Q9HCU5; -.
DR ProteomicsDB; 81801; -.
DR Antibodypedia; 3012; 116 antibodies from 27 providers.
DR DNASU; 10113; -.
DR Ensembl; ENST00000260643.7; ENSP00000260643.2; ENSG00000138073.14.
DR GeneID; 10113; -.
DR KEGG; hsa:10113; -.
DR MANE-Select; ENST00000260643.7; ENSP00000260643.2; NM_013388.6; NP_037520.1.
DR UCSC; uc002rix.3; human.
DR CTD; 10113; -.
DR DisGeNET; 10113; -.
DR GeneCards; PREB; -.
DR HGNC; HGNC:9356; PREB.
DR HPA; ENSG00000138073; Low tissue specificity.
DR MIM; 606395; gene.
DR neXtProt; NX_Q9HCU5; -.
DR OpenTargets; ENSG00000138073; -.
DR PharmGKB; PA33727; -.
DR VEuPathDB; HostDB:ENSG00000138073; -.
DR eggNOG; KOG0771; Eukaryota.
DR GeneTree; ENSGT00390000018031; -.
DR HOGENOM; CLU_054579_1_0_1; -.
DR InParanoid; Q9HCU5; -.
DR OMA; AHCQMYY; -.
DR OrthoDB; 828247at2759; -.
DR PhylomeDB; Q9HCU5; -.
DR TreeFam; TF314383; -.
DR PathwayCommons; Q9HCU5; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR SignaLink; Q9HCU5; -.
DR BioGRID-ORCS; 10113; 722 hits in 1082 CRISPR screens.
DR ChiTaRS; PREB; human.
DR GeneWiki; PREB; -.
DR GenomeRNAi; 10113; -.
DR Pharos; Q9HCU5; Tbio.
DR PRO; PR:Q9HCU5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HCU5; protein.
DR Bgee; ENSG00000138073; Expressed in right lobe of liver and 189 other tissues.
DR ExpressionAtlas; Q9HCU5; baseline and differential.
DR Genevisible; Q9HCU5; HS.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR045260; Sec12-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR PANTHER; PTHR23284; PTHR23284; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Nitration; Nucleus; Protein transport;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix; Transport; WD repeat.
FT CHAIN 1..417
FT /note="Prolactin regulatory element-binding protein"
FT /id="PRO_0000051154"
FT TOPO_DOM 1..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..417
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 4..50
FT /note="WD 1"
FT REPEAT 58..97
FT /note="WD 2"
FT REPEAT 127..183
FT /note="WD 3"
FT REPEAT 187..224
FT /note="WD 4"
FT REPEAT 230..287
FT /note="WD 5"
FT REPEAT 291..329
FT /note="WD 6"
FT REPEAT 334..385
FT /note="WD 7"
FT REGION 101..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUQ2"
FT CONFLICT 19
FT /note="L -> F (in Ref. 1; AAG01692)"
FT /evidence="ECO:0000305"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:5TF2"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5TF2"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5TF2"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:5TF2"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:5TF2"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:5TF2"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5TF2"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:5TF2"
SQ SEQUENCE 417 AA; 45468 MW; 7FD490A641202D19 CRC64;
MGRRRAPELY RAPFPLYALQ VDPSTGLLIA AGGGGAAKTG IKNGVHFLQL ELINGRLSAS
LLHSHDTETR ATMNLALAGD ILAAGQDAHC QLLRFQAHQQ QGNKAEKAGS KEQGPRQRKG
AAPAEKKCGA ETQHEGLELR VENLQAVQTD FSSDPLQKVV CFNHDNTLLA TGGTDGYVRV
WKVPSLEKVL EFKAHEGEIE DLALGPDGKL VTVGRDLKAS VWQKDQLVTQ LHWQENGPTF
SSTPYRYQAC RFGQVPDQPA GLRLFTVQIP HKRLRQPPPC YLTAWDGSNF LPLRTKSCGH
EVVSCLDVSE SGTFLGLGTV TGSVAIYIAF SLQCLYYVRE AHGIVVTDVA FLPEKGRGPE
LLGSHETALF SVAVDSRCQL HLLPSRRSVP VWLLLLLCVG LIIVTILLLQ SAFPGFL
