HPBP1_HUMAN
ID HPBP1_HUMAN Reviewed; 359 AA.
AC Q9NZL4; B3KQP0; B4DG11; O95351; Q6ZNU5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Hsp70-binding protein 1 {ECO:0000305};
DE Short=HspBP1;
DE AltName: Full=Heat shock protein-binding protein 1;
DE AltName: Full=Hsp70-binding protein 2;
DE Short=HspBP2;
DE AltName: Full=Hsp70-interacting protein 1;
DE AltName: Full=Hsp70-interacting protein 2;
GN Name=HSPBP1 {ECO:0000312|HGNC:HGNC:24989}; Synonyms=HSPBP; ORFNames=PP1845;
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), FUNCTION, INTERACTION WITH HSPA1A,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9830037; DOI=10.1074/jbc.273.49.32883;
RA Raynes D.A., Guerriero V. Jr.;
RT "Inhibition of Hsp70 ATPase activity and protein renaturation by a novel
RT Hsp70-binding protein.";
RL J. Biol. Chem. 273:32883-32888(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, POLYMORPHISM OF POLY-GLY
RP REGION, AND VARIANT GLY-GLY-GLY-30 INS.
RC TISSUE=Heart;
RX PubMed=10786638; DOI=10.1016/s0167-4781(99)00238-9;
RA Guerriero V. Jr., Raynes D.A.;
RT "Isolation and characterization of isoforms of HspBP1, inhibitors of
RT Hsp70.";
RL Biochim. Biophys. Acta 1490:203-207(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Tanimura S., Tsujimoto M., Kohno M.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLY-GLY-GLY-30 INS.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP VAL-25 AND GLY-GLY-GLY-30 INS.
RC TISSUE=Amygdala, and Spleen;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLY-GLY-GLY-30 INS.
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLY-GLY-GLY-30 INS.
RC TISSUE=Lung, and 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 [9]
RP FUNCTION, AND INTERACTION WITH HSPA1A.
RX PubMed=12651857; DOI=10.1074/jbc.m301109200;
RA McLellan C.A., Raynes D.A., Guerriero V. Jr.;
RT "HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of
RT altering the conformation of the Hsp70 ATPase domain.";
RL J. Biol. Chem. 278:19017-19022(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH HSPA1A AND STUB1.
RX PubMed=15215316; DOI=10.1091/mbc.e04-04-0293;
RA Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.;
RT "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates
RT the maturation of the cystic fibrosis transmembrane conductance
RT regulator.";
RL Mol. Biol. Cell 15:4003-4010(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP FUNCTION, AND INTERACTION WITH PGLYRP1.
RX PubMed=21247889; DOI=10.1074/jbc.m110.163436;
RA Yashin D.V., Dukhanina E.A., Kabanova O.D., Romanova E.A., Lukyanova T.I.,
RA Tonevitskii A.G., Raynes D.A., Gnuchev N.V., Guerriero V., Georgiev G.P.,
RA Sashchenko L.P.;
RT "The heat shock-binding protein (HspBP1) protects cells against the
RT cytotoxic action of the Tag7-Hsp70 complex.";
RL J. Biol. Chem. 286:10258-10264(2011).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 84-359 IN COMPLEX WITH HSPA1A.
RX PubMed=15694338; DOI=10.1016/j.molcel.2004.12.023;
RA Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C.,
RA Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.;
RT "Regulation of Hsp70 function by HspBP1: structural analysis reveals an
RT alternate mechanism for Hsp70 nucleotide exchange.";
RL Mol. Cell 17:367-379(2005).
CC -!- FUNCTION: Inhibits HSPA1A chaperone activity by changing the
CC conformation of the ATP-binding domain of HSPA1A and interfering with
CC ATP binding. Interferes with ubiquitination mediated by STUB1 and
CC inhibits chaperone-assisted degradation of immature CFTR.
CC {ECO:0000269|PubMed:10786638, ECO:0000269|PubMed:12651857,
CC ECO:0000269|PubMed:15215316, ECO:0000269|PubMed:21247889,
CC ECO:0000269|PubMed:9830037}.
CC -!- SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected in a
CC ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with
CC PGLYRP1; this interaction blocks the cytotoxic activity of the PGLYRP1-
CC HSPA1A complex (PubMed:21247889). {ECO:0000269|PubMed:12651857,
CC ECO:0000269|PubMed:15215316, ECO:0000269|PubMed:15694338,
CC ECO:0000269|PubMed:21247889, ECO:0000269|PubMed:9830037}.
CC -!- INTERACTION:
CC Q9NZL4; P54652: HSPA2; NbExp=7; IntAct=EBI-356763, EBI-356991;
CC Q9NZL4; P11142: HSPA8; NbExp=12; IntAct=EBI-356763, EBI-351896;
CC Q9NZL4; Q96IS6: HSPA8; NbExp=5; IntAct=EBI-356763, EBI-10289199;
CC Q9NZL4; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-356763, EBI-945833;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NZL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZL4-2; Sequence=VSP_015945;
CC Name=3;
CC IsoId=Q9NZL4-3; Sequence=VSP_053681, VSP_053682;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9830037}.
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DR EMBL; AF093420; AAC79703.1; -; mRNA.
DR EMBL; AF187859; AAF35833.1; -; mRNA.
DR EMBL; AB020592; BAB18742.1; -; mRNA.
DR EMBL; AF217996; AAG17238.1; -; mRNA.
DR EMBL; AK130636; BAC85399.1; -; mRNA.
DR EMBL; AK294358; BAG57622.1; -; mRNA.
DR EMBL; CR457118; CAG33399.1; -; mRNA.
DR EMBL; AK075293; BAG52102.1; -; mRNA.
DR EMBL; BC001236; AAH01236.1; -; mRNA.
DR EMBL; BC002373; AAH02373.1; -; mRNA.
DR CCDS; CCDS33111.1; -. [Q9NZL4-1]
DR RefSeq; NP_001123578.1; NM_001130106.1. [Q9NZL4-1]
DR RefSeq; NP_001284529.1; NM_001297600.1.
DR RefSeq; NP_036399.3; NM_012267.4. [Q9NZL4-1]
DR RefSeq; XP_016882033.1; XM_017026544.1. [Q9NZL4-1]
DR PDB; 1XQR; X-ray; 2.10 A; A/B=84-359.
DR PDB; 1XQS; X-ray; 2.90 A; A/B=84-359.
DR PDBsum; 1XQR; -.
DR PDBsum; 1XQS; -.
DR AlphaFoldDB; Q9NZL4; -.
DR SMR; Q9NZL4; -.
DR BioGRID; 117168; 146.
DR IntAct; Q9NZL4; 76.
DR MINT; Q9NZL4; -.
DR STRING; 9606.ENSP00000255631; -.
DR GlyGen; Q9NZL4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZL4; -.
DR MetOSite; Q9NZL4; -.
DR PhosphoSitePlus; Q9NZL4; -.
DR BioMuta; HSPBP1; -.
DR DMDM; 74734730; -.
DR EPD; Q9NZL4; -.
DR jPOST; Q9NZL4; -.
DR MassIVE; Q9NZL4; -.
DR PaxDb; Q9NZL4; -.
DR PeptideAtlas; Q9NZL4; -.
DR PRIDE; Q9NZL4; -.
DR ProteomicsDB; 83428; -. [Q9NZL4-1]
DR ProteomicsDB; 83429; -. [Q9NZL4-2]
DR Antibodypedia; 33053; 311 antibodies from 24 providers.
DR DNASU; 23640; -.
DR Ensembl; ENST00000255631.9; ENSP00000255631.4; ENSG00000133265.11. [Q9NZL4-1]
DR Ensembl; ENST00000433386.7; ENSP00000398244.1; ENSG00000133265.11. [Q9NZL4-1]
DR Ensembl; ENST00000587922.5; ENSP00000467574.1; ENSG00000133265.11. [Q9NZL4-1]
DR GeneID; 23640; -.
DR KEGG; hsa:23640; -.
DR MANE-Select; ENST00000433386.7; ENSP00000398244.1; NM_012267.5; NP_036399.3.
DR UCSC; uc002qkc.4; human. [Q9NZL4-1]
DR CTD; 23640; -.
DR DisGeNET; 23640; -.
DR GeneCards; HSPBP1; -.
DR HGNC; HGNC:24989; HSPBP1.
DR HPA; ENSG00000133265; Low tissue specificity.
DR MIM; 612939; gene.
DR neXtProt; NX_Q9NZL4; -.
DR OpenTargets; ENSG00000133265; -.
DR PharmGKB; PA164720725; -.
DR VEuPathDB; HostDB:ENSG00000133265; -.
DR eggNOG; KOG2160; Eukaryota.
DR GeneTree; ENSGT00940000153909; -.
DR HOGENOM; CLU_049387_0_1_1; -.
DR InParanoid; Q9NZL4; -.
DR OMA; CHVQSGL; -.
DR OrthoDB; 1310125at2759; -.
DR PhylomeDB; Q9NZL4; -.
DR TreeFam; TF324307; -.
DR PathwayCommons; Q9NZL4; -.
DR SignaLink; Q9NZL4; -.
DR BioGRID-ORCS; 23640; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; HSPBP1; human.
DR EvolutionaryTrace; Q9NZL4; -.
DR GeneWiki; HSPBP1; -.
DR GenomeRNAi; 23640; -.
DR Pharos; Q9NZL4; Tbio.
DR PRO; PR:Q9NZL4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NZL4; protein.
DR Bgee; ENSG00000133265; Expressed in nucleus accumbens and 190 other tissues.
DR ExpressionAtlas; Q9NZL4; baseline and differential.
DR Genevisible; Q9NZL4; HS.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013918; Nucleotide_exch_fac_Fes1.
DR Pfam; PF08609; Fes1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..359
FT /note="Hsp70-binding protein 1"
FT /id="PRO_0000084035"
FT REPEAT 132..174
FT /note="ARM 1"
FT REPEAT 177..217
FT /note="ARM 2"
FT REPEAT 220..259
FT /note="ARM 3"
FT REPEAT 262..301
FT /note="ARM 4"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MGGRRAPLKRRLLSRPSRIDPSGRQSCFSGDHLLPLTHSSLLHKRPM
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053681"
FT VAR_SEQ 25..27
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053682"
FT VAR_SEQ 204..306
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015945"
FT VARIANT 25
FT /note="G -> V (in dbSNP:rs140649061)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_080621"
FT VARIANT 30
FT /note="G -> GGGG"
FT /evidence="ECO:0000269|PubMed:10786638,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15498874, ECO:0000269|PubMed:16303743"
FT /id="VAR_023645"
FT CONFLICT 273
FT /note="M -> V (in Ref. 5; BAG57622)"
FT /evidence="ECO:0000305"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 110..131
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:1XQR"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1XQR"
FT HELIX 335..348
FT /evidence="ECO:0007829|PDB:1XQR"
SQ SEQUENCE 359 AA; 39303 MW; 99C3B7ECD4DFAF33 CRC64;
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG SSAGGSGNSR PPRNLQGLLQ MAITAGSEEP
DPPPEPMSEE RRQWLQEAMS AAFRGQREEV EQMKSCLRVL SQPMPPTAGE AEQAADQQER
EGALELLADL CENMDNAADF CQLSGMHLLV GRYLEAGAAG LRWRAAQLIG TCSQNVAAIQ
EQVLGLGALR KLLRLLDRDA CDTVRVKALF AISCLVREQE AGLLQFLRLD GFSVLMRAMQ
QQVQKLKVKS AFLLQNLLVG HPEHKGTLCS MGMVQQLVAL VRTEHSPFHE HVLGALCSLV
TDFPQGVREC REPELGLEEL LRHRCQLLQQ HEEYQEELEF CEKLLQTCFS SPADDSMDR
