STXB5_MOUSE
ID STXB5_MOUSE Reviewed; 1152 AA.
AC Q8K400; E9QLY8; Q80TM5; Q8K401; Q9D2F3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Syntaxin-binding protein 5;
DE AltName: Full=Lethal(2) giant larvae protein homolog 3;
DE AltName: Full=Tomosyn-1;
GN Name=Stxbp5; Synonyms=Kiaa4253, Llgl3;
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), FUNCTION, INTERACTION WITH STX1A
RP AND STX4A, IDENTIFICATION IN A COMPLEX WITH STX4A AND SNAP23, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Swiss albino; TISSUE=Adipocyte;
RX PubMed=12832401; DOI=10.1074/jbc.m304261200;
RA Widberg C.H., Bryant N.J., Girotti M., Rea S., James D.E.;
RT "Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role
RT in insulin-stimulated GLUT4 translocation.";
RL J. Biol. Chem. 278:35093-35101(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 892-1152.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=15659226; DOI=10.1111/j.1471-4159.2004.02890.x;
RA Groffen A.J.A., Jacobsen L., Schut D., Verhage M.;
RT "Two distinct genes drive expression of seven tomosyn isoforms in the
RT mammalian brain, sharing a conserved structure with a unique variable
RT domain.";
RL J. Neurochem. 92:554-568(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783 AND SER-786, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760; SER-783 AND SER-786, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; SER-760; SER-783;
RP THR-785; SER-786; SER-901; SER-903 AND SER-1059, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC 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: Plays a regulatory role in calcium-dependent exocytosis and
CC neurotransmitter release (By similarity). Inhibits membrane fusion
CC between transport vesicles and the plasma membrane. May modulate the
CC assembly of trans-SNARE complexes between transport vesicles and the
CC plasma membrane. Competes with STXBP1 for STX1 binding. Inhibits
CC translocation of GLUT4 from intracellular vesicles to the plasma
CC membrane. {ECO:0000250, ECO:0000269|PubMed:12832401}.
CC -!- SUBUNIT: Part of a complex that contains STX1, STXBP5, SNAP25 and SYT1
CC (By similarity). Interacts with STX1A and STX4A via its v-SNARE
CC homology domain. Part of a complex that contains STXBP5, STX4A and
CC SNAP23. {ECO:0000250, ECO:0000269|PubMed:12832401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12832401}. Cell
CC membrane {ECO:0000269|PubMed:12832401}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12832401}. Membrane {ECO:0000269|PubMed:12832401};
CC Peripheral membrane protein {ECO:0000269|PubMed:12832401}.
CC Note=Cytoplasmic, and associated with vesicular membranes and the
CC plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K400-2; Sequence=VSP_016206;
CC -!- TISSUE SPECIFICITY: Detected in heart, spleen, lung, skeletal muscle,
CC liver and kidney (at protein level). Detected in brain, particularly in
CC the olfactory bulb and in hippocampus. Detected in the tenia tecta and
CC in the piriform layer of the brain cortex.
CC {ECO:0000269|PubMed:12832401, ECO:0000269|PubMed:15659226}.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
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DR EMBL; AF516607; AAM61881.1; -; mRNA.
DR EMBL; AF516608; AAM61882.1; -; mRNA.
DR EMBL; AK019788; BAB31853.1; -; mRNA.
DR EMBL; AC122390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122417; BAC65699.1; -; mRNA.
DR RefSeq; XP_006512989.1; XM_006512926.3. [Q8K400-1]
DR AlphaFoldDB; Q8K400; -.
DR SMR; Q8K400; -.
DR BioGRID; 219650; 3.
DR IntAct; Q8K400; 2.
DR MINT; Q8K400; -.
DR STRING; 10090.ENSMUSP00000123253; -.
DR iPTMnet; Q8K400; -.
DR PhosphoSitePlus; Q8K400; -.
DR SwissPalm; Q8K400; -.
DR EPD; Q8K400; -.
DR jPOST; Q8K400; -.
DR MaxQB; Q8K400; -.
DR PaxDb; Q8K400; -.
DR PeptideAtlas; Q8K400; -.
DR PRIDE; Q8K400; -.
DR ProteomicsDB; 254778; -. [Q8K400-1]
DR ProteomicsDB; 254779; -. [Q8K400-2]
DR Antibodypedia; 33249; 52 antibodies from 14 providers.
DR Ensembl; ENSMUST00000038213; ENSMUSP00000044535; ENSMUSG00000019790. [Q8K400-1]
DR GeneID; 78808; -.
DR UCSC; uc007eiy.1; mouse. [Q8K400-2]
DR UCSC; uc007eja.1; mouse. [Q8K400-1]
DR CTD; 134957; -.
DR MGI; MGI:1926058; Stxbp5.
DR VEuPathDB; HostDB:ENSMUSG00000019790; -.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00950000182906; -.
DR InParanoid; Q8K400; -.
DR OrthoDB; 84844at2759; -.
DR PhylomeDB; Q8K400; -.
DR BioGRID-ORCS; 78808; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Stxbp5; mouse.
DR PRO; PR:Q8K400; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K400; protein.
DR Bgee; ENSMUSG00000019790; Expressed in animal zygote and 217 other tissues.
DR ExpressionAtlas; Q8K400; baseline and differential.
DR Genevisible; Q8K400; MM.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098674; C:extrinsic component of neuronal dense core vesicle membrane; IDA:SynGO.
DR GO; GO:0098888; C:extrinsic component of presynaptic membrane; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; NAS:BHF-UCL.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:BHF-UCL.
DR GO; GO:0007409; P:axonogenesis; TAS:BHF-UCL.
DR GO; GO:0006887; P:exocytosis; IDA:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; IDA:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IDA:SynGO.
DR GO; GO:0099504; P:synaptic vesicle cycle; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR000664; Lethal2_giant.
DR InterPro; IPR013905; Lgl_C_dom.
DR InterPro; IPR013577; LLGL2.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08596; Lgl_C; 1.
DR Pfam; PF08366; LLGL; 1.
DR Pfam; PF00400; WD40; 1.
DR PRINTS; PR00962; LETHAL2GIANT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50892; V_SNARE; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Exocytosis;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport; WD repeat.
FT CHAIN 1..1152
FT /note="Syntaxin-binding protein 5"
FT /id="PRO_0000051245"
FT REPEAT 62..95
FT /note="WD 1"
FT REPEAT 102..141
FT /note="WD 2"
FT REPEAT 146..182
FT /note="WD 3"
FT REPEAT 201..235
FT /note="WD 4"
FT REPEAT 241..273
FT /note="WD 5"
FT REPEAT 295..337
FT /note="WD 6"
FT REPEAT 345..379
FT /note="WD 7"
FT REPEAT 401..478
FT /note="WD 8"
FT REPEAT 506..620
FT /note="WD 9"
FT REPEAT 634..696
FT /note="WD 10"
FT REPEAT 795..852
FT /note="WD 11"
FT REPEAT 861..935
FT /note="WD 12"
FT REPEAT 940..984
FT /note="WD 13"
FT REPEAT 998..1021
FT /note="WD 14"
FT DOMAIN 1087..1147
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 14..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 763
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 785
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1040
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT VAR_SEQ 1..754
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016206"
FT CONFLICT 90
FT /note="V -> A (in Ref. 1; AAM61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="A -> S (in Ref. 1; AAM61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="L -> P (in Ref. 1; AAM61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="D -> E (in Ref. 1; AAM61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="D -> G (in Ref. 1; AAM61881)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="H -> Y (in Ref. 1; AAM61881)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="A -> T (in Ref. 1; AAM61881)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="L -> F (in Ref. 1; AAM61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="S -> F (in Ref. 3; BAB31853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1152 AA; 127651 MW; CB62642C7BE5F376 CRC64;
MRKFNIRKVL DGLTAGSSSA SQQQQQQQHP PGNREPEIQE TLQSEHFQLC KTVRHGFPYQ
PSALAFDPVQ KILAVGTQTG ALRLFGRPGV ECYCQHDSGA AVIQLQFLIN EGALVSALAD
DTLHLWNLRQ KRPAVLHSLK FCRERVTFCH LPFQSKWLYV GTERGNIHIV NVESFTLSGY
VIMWNKAIEL SSKAHPGPVV HISDNPMDEG KLLIGFESGT VVLWDLKSKK ADYRYTYDEA
IHSVAWHHEG KQFICSHSDG TLTIWNVRSP AKPVQTITPH GKQLKDGKKP EPCKPILKVE
LKTTRSGEPF IILSGGLSYD TVGRRPCLTV MHGKSTAVLE MDYSIVDFLT LCETPYPNDF
QEPYAVVVLL EKDLVLIDLA QNGYPIFENP YPLSIHESPV TCCEYFADCP VDLIPALYSV
GARQKRQGYS KKEWPINGGN WGLGAQSYPE IIITGHADGS VKFWDASAIT LQVLYKLKTS
KVFEKSRNKD DRQNTDIVDE DPYAIQIISW CPESRMLCIA GVSAHVIIYR FSKQEVLTEV
IPMLEVRLLY EINDVDTPEG EQPPPLSTPV GSSNPQPIPP QSHPSTSSSS SDGLRDNVPC
LKVKNSPLKQ SPGYQTELVI QLVWVGGEPP QQITSLALNS SYGLVVFGNC NGIAMVDYLQ
KAVLLNLSTI ELYGSNDPYR REPRSPRKSR QPSGAGLCDI TEGTVVPEDR CKSPTSGSSS
PHNSDDEQKV NNFIEKVKTQ SRKFSKMVAN DLAKMSRKLS LPTDLKPDLD VKDNSFSRSR
SSSVTSIDKE SRETISALHF CETLTRKADS SPSPCLWVGT TVGTAFVITL NLPPGPEQRL
LQPVIVSPSG TILRLKGAIL RMAFLDATGC LMSPAYEPWK EHNVAEEKDE KEKLKKRRPV
SVSPSSSQEI SENQYAVICS EKQAKVMSLP TQSCAYKQNI TETSFVLRGD IVALSNSVCL
ACFCANGHIM TFSLPSLRPL LDVYYLPLTN MRIARTFCFA NNGQALYLVS PTEIQRLTYS
QETCENLQEM LGELFTPVET PEAPNRGFFK GLFGGGAQSL DREELFGESS SGKASRSLAQ
HIPGPGGIEG VKGAASGVVG ELARARLALD ERGQKLSDLE ERTAAMMSSA DSFSKHAHEM
MLKYKDKKWY QF
