STXB3_MOUSE
ID STXB3_MOUSE Reviewed; 592 AA.
AC Q60770; Q3TE73; Q3U2S2; Q3U8D9; Q3UA91; Q3UUB0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Syntaxin-binding protein 3;
DE AltName: Full=MUNC-18-3;
DE AltName: Full=Mammalian homolog of Unc-18c;
DE Short=Munc-18c;
DE AltName: Full=Protein unc-18 homolog 3;
DE Short=Unc18-3;
DE AltName: Full=Protein unc-18 homolog C;
DE Short=Unc-18C;
GN Name=Stxbp3; Synonyms=Stxbp3a, Unc18c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Adipocyte;
RX PubMed=7890715; DOI=10.1074/jbc.270.11.5857;
RA Tellam J.T., McIntosh S., James D.E.;
RT "Molecular identification of two novel Munc-18 isoforms expressed in non-
RT neuronal tissues.";
RL J. Biol. Chem. 270:5857-5863(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8824310; DOI=10.1523/jneurosci.16-21-06695.1996;
RA Gengyo-Ando K., Kitayama H., Mukaida M., Ikawa Y.;
RT "A murine neural-specific homolog corrects cholinergic defects in
RT Caenorhabditis elegans unc-18 mutants.";
RL J. Neurosci. 16:6695-6702(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow macrophage, Dendritic cell, Spinal cord, Thymocyte, and
RC Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, INTERACTION WITH STX4, AND SUBCELLULAR LOCATION.
RX PubMed=9045631; DOI=10.1074/jbc.272.10.6179;
RA Tellam J.T., Macaulay S.L., McIntosh S., Hewish D.R., Ward C.W.,
RA James D.E.;
RT "Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative
RT role in insulin-dependent movement of GLUT-4.";
RL J. Biol. Chem. 272:6179-6186(1997).
RN [7]
RP INTERACTION WITH DOC2B AND STX4.
RX PubMed=17548353; DOI=10.1074/jbc.m701661200;
RA Ke B., Oh E., Thurmond D.C.;
RT "Doc2beta is a novel Munc18c-interacting partner and positive effector of
RT syntaxin 4-mediated exocytosis.";
RL J. Biol. Chem. 282:21786-21797(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Together with STX4 and VAMP2, may play a role in insulin-
CC dependent movement of GLUT4 and in docking/fusion of intracellular
CC GLUT4-containing vesicles with the cell surface in adipocytes.
CC {ECO:0000269|PubMed:9045631}.
CC -!- SUBUNIT: Interacts with STX4. Interacts with DOC2B; the interaction is
CC direct, occurs at the cell membrane, excludes interaction with STX4 and
CC regulates glucose-stimulated insulin secretion.
CC {ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:9045631}.
CC -!- INTERACTION:
CC Q60770; Q08850: Stx4; Xeno; NbExp=4; IntAct=EBI-8430169, EBI-918243;
CC Q60770; P63045: Vamp2; Xeno; NbExp=2; IntAct=EBI-8430169, EBI-520880;
CC Q60770-1; P70452: Stx4; NbExp=3; IntAct=EBI-15639434, EBI-645716;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:9045631}. Note=In platelets, predominantly
CC cytosolic. Low amounts membrane-associated (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60770-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60770-2; Sequence=VSP_037061, VSP_037062;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested.
CC {ECO:0000269|PubMed:8824310}.
CC -!- PTM: Phosphorylated by PKC in platelets in response to thrombin
CC stimulation; phosphorylation inhibits binding to STX4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE41375.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U19521; AAA69913.1; -; mRNA.
DR EMBL; D30798; BAA19478.1; -; mRNA.
DR EMBL; AK138609; BAE23717.1; -; mRNA.
DR EMBL; AK151466; BAE30424.1; -; mRNA.
DR EMBL; AK152261; BAE31079.1; -; mRNA.
DR EMBL; AK155133; BAE33068.1; -; mRNA.
DR EMBL; AK169799; BAE41375.1; ALT_FRAME; mRNA.
DR EMBL; AL671894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062901; AAH62901.1; -; mRNA.
DR CCDS; CCDS17768.1; -. [Q60770-1]
DR PIR; I49239; I49239.
DR RefSeq; NP_035634.1; NM_011504.1. [Q60770-1]
DR PDB; 3PUK; X-ray; 3.05 A; A/B=1-592.
DR PDBsum; 3PUK; -.
DR AlphaFoldDB; Q60770; -.
DR SMR; Q60770; -.
DR BioGRID; 203566; 8.
DR DIP; DIP-60305N; -.
DR IntAct; Q60770; 8.
DR STRING; 10090.ENSMUSP00000099681; -.
DR iPTMnet; Q60770; -.
DR PhosphoSitePlus; Q60770; -.
DR SwissPalm; Q60770; -.
DR EPD; Q60770; -.
DR jPOST; Q60770; -.
DR MaxQB; Q60770; -.
DR PaxDb; Q60770; -.
DR PeptideAtlas; Q60770; -.
DR PRIDE; Q60770; -.
DR ProteomicsDB; 257097; -. [Q60770-1]
DR ProteomicsDB; 257098; -. [Q60770-2]
DR Antibodypedia; 20045; 232 antibodies from 30 providers.
DR DNASU; 20912; -.
DR Ensembl; ENSMUST00000102621; ENSMUSP00000099681; ENSMUSG00000027882. [Q60770-1]
DR GeneID; 20912; -.
DR KEGG; mmu:20912; -.
DR UCSC; uc008qzr.3; mouse. [Q60770-1]
DR CTD; 6814; -.
DR MGI; MGI:107362; Stxbp3.
DR VEuPathDB; HostDB:ENSMUSG00000027882; -.
DR eggNOG; KOG1300; Eukaryota.
DR GeneTree; ENSGT00940000157607; -.
DR HOGENOM; CLU_009210_2_1_1; -.
DR InParanoid; Q60770; -.
DR OMA; SKGPMET; -.
DR OrthoDB; 725424at2759; -.
DR PhylomeDB; Q60770; -.
DR TreeFam; TF313242; -.
DR Reactome; R-MMU-114516; Disinhibition of SNARE formation.
DR BioGRID-ORCS; 20912; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Stxbp3; mouse.
DR EvolutionaryTrace; Q60770; -.
DR PRO; PR:Q60770; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q60770; protein.
DR Bgee; ENSMUSG00000027882; Expressed in placenta labyrinth and 256 other tissues.
DR ExpressionAtlas; Q60770; baseline and differential.
DR Genevisible; Q60770; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0070820; C:tertiary granule; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; IDA:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0001678; P:cellular glucose homeostasis; IDA:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; ISO:MGI.
DR GO; GO:0046325; P:negative regulation of glucose import; IDA:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0043312; P:neutrophil degranulation; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0022615; P:protein to membrane docking; IMP:MGI.
DR GO; GO:0032868; P:response to insulin; IDA:MGI.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..592
FT /note="Syntaxin-binding protein 3"
FT /id="PRO_0000206286"
FT REGION 1..255
FT /note="Mediates interaction with DOC2B"
FT /evidence="ECO:0000269|PubMed:17548353"
FT VAR_SEQ 344..370
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037061"
FT VAR_SEQ 484..511
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037062"
FT CONFLICT 123
FT /note="K -> R (in Ref. 3; BAE31079)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="N -> Y (in Ref. 3; BAE23717)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="E -> Q (in Ref. 3; BAE33068)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="N -> S (in Ref. 3; BAE33068)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="E -> G (in Ref. 3; BAE23717)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="R -> K (in Ref. 3; BAE31079)"
FT /evidence="ECO:0000305"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 168..188
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3PUK"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3PUK"
FT TURN 289..294
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:3PUK"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:3PUK"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 340..360
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 362..373
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:3PUK"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:3PUK"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 479..486
FT /evidence="ECO:0007829|PDB:3PUK"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 530..537
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 542..554
FT /evidence="ECO:0007829|PDB:3PUK"
FT STRAND 557..568
FT /evidence="ECO:0007829|PDB:3PUK"
FT HELIX 570..577
FT /evidence="ECO:0007829|PDB:3PUK"
SQ SEQUENCE 592 AA; 67942 MW; 7874B71DE107871A CRC64;
MAPPVSERGL KSVVWRKIKT AVFDDCRKEG EWKIMLLDEF TTKLLSSCCK MTDLLEEGIT
VIENIYKNRE PVRQMKALYF ISPTPKSVDC FLRDFGSKSE KKYKAAYIYF TDFCPDSLFN
KIKASCSKSI RRCKEINISF IPQESQVYTL DVPDAFYYCY SPDPSNASRK EVVMEAMAEQ
IVTVCATLDE NPGVRYKSKP LDNASKLAQL VEKKLEDYYK IDEKGLIKGK TQSQLLIIDR
GFDPVSTVLH ELTFQAMAYD LLPIENDTYK YKTDGKEKEA VLEEDDDLWV RVRHRHIAVV
LEEIPKLMKE ISSTKKATEG KTSLSALTQL MKKMPHFRKQ ISKQVVHLNL AEDCMNKFKL
NIEKLCKTEQ DLALGTDAEG QRVKDSMLVL LPVLLNKNHD NCDKIRAVLL YIFGINGTTE
ENLDRLIHNV KIEDDSDMIR NWSHLGVPIV PPSQQAKPLR KDRSAEETFQ LSRWTPFIKD
IMEDAIDNRL DSKEWPYCSR CPAVWNGSGA VSARQKPRTN YLELDRKNGS RLIIFVIGGI
TYSEMRCAYE VSQAHKSCEV IIGSTHILTP RKLLDDIKML NKSKDKVSFK DE
