HS105_MOUSE
ID HS105_MOUSE Reviewed; 858 AA.
AC Q61699; Q3TNS2; Q3UIY8; Q62578; Q62579; Q6A0A5; Q8C430; Q8VCW6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Heat shock protein 105 kDa;
DE AltName: Full=42 degrees C-HSP;
DE AltName: Full=Heat shock 110 kDa protein;
DE AltName: Full=Heat shock-related 100 kDa protein E7I;
DE Short=HSP-E7I;
GN Name=Hsph1; Synonyms=Hsp105, Hsp110, Kiaa0201;
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 HSP105-ALPHA).
RX PubMed=7556594; DOI=10.1016/0014-5793(95)00884-c;
RA Morozov A., Subjeck J., Raychaudhuri P.;
RT "HPV16 E7 oncoprotein induces expression of a 110 kDa heat shock protein.";
RL FEBS Lett. 371:214-218(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HSP105-ALPHA AND HSP105-BETA).
RX PubMed=8530361; DOI=10.1074/jbc.270.50.29718;
RA Yasuda K., Nakai A., Hatayama T., Nagata K.;
RT "Cloning and expression of murine high molecular mass heat shock proteins,
RT HSP105.";
RL J. Biol. Chem. 270:29718-29723(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP HSP105-ALPHA).
RC STRAIN=BALB/cJ;
RX PubMed=10066425; DOI=10.1006/bbrc.1999.0283;
RA Yasuda K., Ishihara K., Nakashima K., Hatayama T.;
RT "Genomic cloning and promoter analysis of the mouse 105-kDa heat shock
RT protein (HSP105) gene.";
RL Biochem. Biophys. Res. Commun. 256:75-80(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HSP105-ALPHA).
RC STRAIN=C57BL/6J; TISSUE=Eye, Hippocampus, and Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HSP105-ALPHA).
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 54-68; 74-82; 361-374 AND 462-471, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-858.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [8]
RP INTERACTION WITH HSPA8.
RX PubMed=9675148; DOI=10.1006/bbrc.1998.8979;
RA Hatayama T., Yasuda K., Yasuda K.;
RT "Association of HSP105 with HSC70 in high molecular mass complexes in mouse
RT FM3A cells.";
RL Biochem. Biophys. Res. Commun. 248:395-401(1998).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=10772927; DOI=10.1006/bbrc.2000.2541;
RA Ishihara K., Yasuda K., Hatayama T.;
RT "Phosphorylation of the 105-kDa heat shock proteins, HSP105alpha and
RT HSP105beta, by casein kinase II.";
RL Biochem. Biophys. Res. Commun. 270:927-931(2000).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10865058; DOI=10.1016/s0006-8993(00)02346-5;
RA Hylander B.L., Chen X., Graf P.C.F., Subjeck J.R.;
RT "The distribution and localization of hsp110 in brain.";
RL Brain Res. 869:49-55(2000).
RN [11]
RP PHOSPHORYLATION AT SER-509.
RX PubMed=12558502; DOI=10.1042/bj20021331;
RA Ishihara K., Yamagishi N., Hatayama T.;
RT "Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its
RT function.";
RL Biochem. J. 371:917-925(2003).
RN [12]
RP FUNCTION.
RX PubMed=14644449; DOI=10.1016/s0014-5793(03)01292-4;
RA Yamagishi N., Ishihara K., Saito Y., Hatayama T.;
RT "Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-
RT denatured protein in the presence of ADP.";
RL FEBS Lett. 555:390-396(2003).
RN [13]
RP INTERACTION WITH HSPA8, AND FUNCTION.
RX PubMed=15292236; DOI=10.1074/jbc.m407947200;
RA Yamagishi N., Ishihara K., Hatayama T.;
RT "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase
RT activity.";
RL J. Biol. Chem. 279:41727-41733(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=16232202; DOI=10.1111/j.1349-7006.2005.00093.x;
RA Miyazaki M., Nakatsura T., Yokomine K., Senju S., Monji M., Hosaka S.,
RA Komori H., Yoshitake Y., Motomura Y., Minohara M., Kubo T., Ishihara K.,
RA Hatayama T., Ogawa M., Nishimura Y.;
RT "DNA vaccination of HSP105 leads to tumor rejection of colorectal cancer
RT and melanoma in mice through activation of both CD4 T cells and CD8 T
RT cells.";
RL Cancer Sci. 96:695-705(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-510, AND
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).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Acts as a nucleotide-exchange factor (NEF) for chaperone
CC proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B
CC thereby triggering client/substrate protein release (By similarity).
CC Prevents the aggregation of denatured proteins in cells under severe
CC stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70
CC ATPase and chaperone activities (PubMed:14644449, PubMed:15292236).
CC {ECO:0000250|UniProtKB:Q92598, ECO:0000269|PubMed:14644449,
CC ECO:0000269|PubMed:15292236}.
CC -!- SUBUNIT: Interacts with HSPA8/HSC70 (PubMed:15292236, PubMed:9675148).
CC Interacts with HSPA1A (via NBD) and HSPA1B (via NBD) (By similarity).
CC {ECO:0000250|UniProtKB:Q92598, ECO:0000269|PubMed:15292236,
CC ECO:0000269|PubMed:9675148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10865058}. Nucleus
CC {ECO:0000269|PubMed:10865058}. Note=Strictly cytoplasmic in neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HSP105-alpha;
CC IsoId=Q61699-1; Sequence=Displayed;
CC Name=HSP105-beta;
CC IsoId=Q61699-2; Sequence=VSP_002429;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Present at lower levels
CC in most brain regions, except cerebellum. Within the brain, expression
CC is restricted to neurons (at protein level). Overexpressed in cancer
CC cells. {ECO:0000269|PubMed:10865058, ECO:0000269|PubMed:16232202}.
CC -!- INDUCTION: By heat shock. Hsp105-alpha also induced by other stresses.
CC -!- PTM: Phosphorylation on Ser-509 may be important for regulation of the
CC HSPA8/HSC70 chaperone activity. {ECO:0000269|PubMed:10772927,
CC ECO:0000269|PubMed:12558502}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; L40406; AAA99485.1; -; mRNA.
DR EMBL; D67016; BAA11035.1; -; mRNA.
DR EMBL; D67017; BAA11036.1; -; mRNA.
DR EMBL; AB005282; BAA74540.1; -; Genomic_DNA.
DR EMBL; AK083179; BAC38797.1; -; mRNA.
DR EMBL; AK146697; BAE27367.1; -; mRNA.
DR EMBL; AK165046; BAE38016.1; -; mRNA.
DR EMBL; BC018378; AAH18378.1; -; mRNA.
DR EMBL; AK172913; BAD32191.1; -; mRNA.
DR CCDS; CCDS19885.1; -. [Q61699-1]
DR CCDS; CCDS85010.1; -. [Q61699-2]
DR PIR; S66666; S66666.
DR RefSeq; NP_001334463.1; NM_001347534.1. [Q61699-2]
DR RefSeq; NP_038587.2; NM_013559.2. [Q61699-1]
DR AlphaFoldDB; Q61699; -.
DR SMR; Q61699; -.
DR BioGRID; 200448; 53.
DR CORUM; Q61699; -.
DR DIP; DIP-32354N; -.
DR IntAct; Q61699; 27.
DR MINT; Q61699; -.
DR STRING; 10090.ENSMUSP00000074392; -.
DR iPTMnet; Q61699; -.
DR PhosphoSitePlus; Q61699; -.
DR SwissPalm; Q61699; -.
DR EPD; Q61699; -.
DR jPOST; Q61699; -.
DR MaxQB; Q61699; -.
DR PaxDb; Q61699; -.
DR PeptideAtlas; Q61699; -.
DR PRIDE; Q61699; -.
DR ProteomicsDB; 273137; -. [Q61699-1]
DR ProteomicsDB; 273138; -. [Q61699-2]
DR Antibodypedia; 22778; 534 antibodies from 39 providers.
DR DNASU; 15505; -.
DR Ensembl; ENSMUST00000074846; ENSMUSP00000074392; ENSMUSG00000029657. [Q61699-2]
DR Ensembl; ENSMUST00000201452; ENSMUSP00000144654; ENSMUSG00000029657. [Q61699-1]
DR Ensembl; ENSMUST00000202361; ENSMUSP00000144413; ENSMUSG00000029657. [Q61699-1]
DR GeneID; 15505; -.
DR KEGG; mmu:15505; -.
DR UCSC; uc009apy.1; mouse. [Q61699-1]
DR UCSC; uc009apz.1; mouse. [Q61699-2]
DR CTD; 10808; -.
DR MGI; MGI:105053; Hsph1.
DR VEuPathDB; HostDB:ENSMUSG00000029657; -.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000159635; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; Q61699; -.
DR OMA; NMLSHAY; -.
DR OrthoDB; 406172at2759; -.
DR PhylomeDB; Q61699; -.
DR TreeFam; TF105043; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 15505; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Hsph1; mouse.
DR PRO; PR:Q61699; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61699; protein.
DR Bgee; ENSMUSG00000029657; Expressed in embryonic post-anal tail and 262 other tissues.
DR ExpressionAtlas; Q61699; baseline and differential.
DR Genevisible; Q61699; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; TAS:BHF-UCL.
DR GO; GO:0045345; P:positive regulation of MHC class I biosynthetic process; TAS:BHF-UCL.
DR GO; GO:0051135; P:positive regulation of NK T cell activation; TAS:BHF-UCL.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; NAS:BHF-UCL.
DR GO; GO:0006986; P:response to unfolded protein; TAS:BHF-UCL.
DR CDD; cd11739; HSPH1_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 2.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR042053; HSPH1_NBD.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT CHAIN 2..858
FT /note="Heat shock protein 105 kDa"
FT /id="PRO_0000078285"
FT REGION 500..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 471
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12558502,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 816
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT VAR_SEQ 530..573
FT /note="Missing (in isoform HSP105-beta)"
FT /evidence="ECO:0000303|PubMed:8530361"
FT /id="VSP_002429"
FT CONFLICT 2
FT /note="S -> L (in Ref. 4; BAC38797)"
FT /evidence="ECO:0000305"
FT CONFLICT 7..8
FT /note="DV -> EL (in Ref. 1; AAA99485)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="D -> N (in Ref. 4; BAC38797)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="S -> R (in Ref. 4; BAC38797)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..19
FT /note="AVAR -> VGEG (in Ref. 4; BAC38797)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="E -> D (in Ref. 4; BAC38797)"
FT /evidence="ECO:0000305"
FT CONFLICT 28..29
FT /note="NE -> KD (in Ref. 4; BAC38797)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> R (in Ref. 1; AAA99485 and 2; BAA11036)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="C -> S (in Ref. 4; BAE38016)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="P -> L (in Ref. 2; BAA11036)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="A -> R (in Ref. 1; AAA99485)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="P -> FQ (in Ref. 1; AAA99485)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="I -> R (in Ref. 4; BAE27367)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="I -> N (in Ref. 1; AAA99485)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="A -> R (in Ref. 1; AAA99485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 96407 MW; 0576A4C2C4715032 CRC64;
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA
NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEEH FFSVEQITAM
LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
YGIYKQDLPN AEEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL
VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK
MNRSQFEELC AELLQKIEVP LHSLMAQTQL KAEDVSAIEI VGGATRIPAV KERIAKFFGK
DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV
KVRVNTHGIF TISTASMVEK VPTEEEDGSS LEADMECPNQ RPTESSDVDK NIQQDNSEAG
TQPQVQTDGQ QTSQSPPSPE LTSEESKTPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE
ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE
QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPKVLEEL
GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLDQDPV
VRTHEIRAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NIDKKEDLEG KNNLGAEAPH
QNGECHPNEK GSVNMDLD
