BST1_HUMAN
ID BST1_HUMAN Reviewed; 318 AA.
AC Q10588; B2R6A2; Q1XII0; Q5U0K0; Q96EN3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2;
DE EC=3.2.2.6;
DE AltName: Full=ADP-ribosyl cyclase 2;
DE AltName: Full=Bone marrow stromal antigen 1;
DE Short=BST-1;
DE AltName: Full=Cyclic ADP-ribose hydrolase 2;
DE Short=cADPr hydrolase 2;
DE AltName: CD_antigen=CD157;
DE Flags: Precursor;
GN Name=BST1;
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).
RX PubMed=8202488; DOI=10.1073/pnas.91.12.5325;
RA Kaisho T., Ishikawa J., Oritani K., Inazawa J., Tomizawa H., Muraoka O.,
RA Ochi T., Hirano T.;
RT "BST-1, a surface molecule of bone marrow stromal cell lines that
RT facilitates pre-B-cell growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5325-5329(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Tabata Y., Hayashi A., Mitsuyama M., Kanai S., Furuya T., Saito T.;
RT "BST1 mRNA, nirs splice variant 1.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thalamus;
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.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-297, AND FUNCTION.
RX PubMed=11866528; DOI=10.1006/jmbi.2001.5386;
RA Yamamoto-Katayama S., Ariyoshi M., Ishihara K., Hirano T., Jingami H.,
RA Morikawa K.;
RT "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and
RT NAD glycohydrolase activities.";
RL J. Mol. Biol. 316:711-723(2002).
CC -!- FUNCTION: Synthesizes the second messengers cyclic ADP-ribose and
CC nicotinate-adenine dinucleotide phosphate, the former a second
CC messenger that elicits calcium release from intracellular stores. May
CC be involved in pre-B-cell growth. {ECO:0000269|PubMed:11866528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q10588-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q10588-2; Sequence=VSP_055507;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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DR EMBL; D21878; BAA04885.1; -; mRNA.
DR EMBL; AB175627; BAE92566.1; -; mRNA.
DR EMBL; BT019502; AAV38309.1; -; mRNA.
DR EMBL; AK312497; BAG35399.1; -; mRNA.
DR EMBL; AC114744; AAY40930.1; -; Genomic_DNA.
DR EMBL; CH471069; EAW92744.1; -; Genomic_DNA.
DR EMBL; BC012095; AAH12095.1; -; mRNA.
DR CCDS; CCDS3416.1; -. [Q10588-1]
DR PIR; I59301; I59301.
DR RefSeq; NP_004325.2; NM_004334.2. [Q10588-1]
DR RefSeq; XP_011512183.1; XM_011513881.2. [Q10588-2]
DR PDB; 1ISF; X-ray; 2.50 A; A/B=33-297.
DR PDB; 1ISG; X-ray; 2.60 A; A/B=33-297.
DR PDB; 1ISH; X-ray; 2.40 A; A/B=33-297.
DR PDB; 1ISI; X-ray; 2.10 A; A/B=33-297.
DR PDB; 1ISJ; X-ray; 2.30 A; A/B=33-297.
DR PDB; 1ISM; X-ray; 3.00 A; A/B=33-297.
DR PDBsum; 1ISF; -.
DR PDBsum; 1ISG; -.
DR PDBsum; 1ISH; -.
DR PDBsum; 1ISI; -.
DR PDBsum; 1ISJ; -.
DR PDBsum; 1ISM; -.
DR AlphaFoldDB; Q10588; -.
DR SMR; Q10588; -.
DR BioGRID; 107148; 36.
DR IntAct; Q10588; 1.
DR STRING; 9606.ENSP00000265016; -.
DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
DR DrugBank; DB02483; Etheno-NAD.
DR DrugBank; DB03732; Etheno-Nadp.
DR DrugBank; DB02701; Nicotinamide.
DR DrugBank; DB03227; Nicotinamide Mononucleotide.
DR GlyConnect; 2017; 3 N-Linked glycans (2 sites).
DR GlyGen; Q10588; 4 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q10588; -.
DR PhosphoSitePlus; Q10588; -.
DR BioMuta; BST1; -.
DR DMDM; 116241273; -.
DR CPTAC; CPTAC-2598; -.
DR jPOST; Q10588; -.
DR MassIVE; Q10588; -.
DR MaxQB; Q10588; -.
DR PaxDb; Q10588; -.
DR PeptideAtlas; Q10588; -.
DR PRIDE; Q10588; -.
DR ProteomicsDB; 58865; -. [Q10588-1]
DR ABCD; Q10588; 4 sequenced antibodies.
DR Antibodypedia; 22988; 503 antibodies from 35 providers.
DR DNASU; 683; -.
DR Ensembl; ENST00000265016.9; ENSP00000265016.4; ENSG00000109743.11. [Q10588-1]
DR GeneID; 683; -.
DR KEGG; hsa:683; -.
DR MANE-Select; ENST00000265016.9; ENSP00000265016.4; NM_004334.3; NP_004325.2.
DR UCSC; uc003goh.4; human. [Q10588-1]
DR CTD; 683; -.
DR DisGeNET; 683; -.
DR GeneCards; BST1; -.
DR HGNC; HGNC:1118; BST1.
DR HPA; ENSG00000109743; Group enriched (bone marrow, intestine).
DR MIM; 600387; gene.
DR neXtProt; NX_Q10588; -.
DR OpenTargets; ENSG00000109743; -.
DR PharmGKB; PA25435; -.
DR VEuPathDB; HostDB:ENSG00000109743; -.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR GeneTree; ENSGT00390000017291; -.
DR HOGENOM; CLU_067834_1_0_1; -.
DR InParanoid; Q10588; -.
DR OMA; EPKGAYP; -.
DR OrthoDB; 1460460at2759; -.
DR PhylomeDB; Q10588; -.
DR TreeFam; TF332530; -.
DR PathwayCommons; Q10588; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q10588; -.
DR SIGNOR; Q10588; -.
DR BioGRID-ORCS; 683; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; BST1; human.
DR EvolutionaryTrace; Q10588; -.
DR GeneWiki; BST1; -.
DR GenomeRNAi; 683; -.
DR Pharos; Q10588; Tbio.
DR PRO; PR:Q10588; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q10588; protein.
DR Bgee; ENSG00000109743; Expressed in monocyte and 112 other tissues.
DR ExpressionAtlas; Q10588; baseline and differential.
DR Genevisible; Q10588; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0001931; C:uropod; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061811; F:ADP-ribosyl cyclase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061812; F:cyclic ADP-ribose hydrolase; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IBA:GO_Central.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006959; P:humoral immune response; IC:ParkinsonsUK-UCL.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0002691; P:regulation of cellular extravasation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:ParkinsonsUK-UCL.
DR GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090322; P:regulation of superoxide metabolic process; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ParkinsonsUK-UCL.
DR CDD; cd04759; Rib_hydrolase; 1.
DR InterPro; IPR003193; ADP-ribosyl_cyclase.
DR PANTHER; PTHR10912; PTHR10912; 1.
DR Pfam; PF02267; Rib_hydrolayse; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; NAD; NADP;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..293
FT /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2"
FT /id="PRO_0000004032"
FT PROPEP 294..318
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000004033"
FT SITE 109
FT /note="Crucial for NAD binding and catalysis"
FT SITE 172
FT /note="Crucial for NAD binding and catalysis"
FT SITE 210
FT /note="Crucial for NAD binding and catalysis"
FT LIPID 293
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 51..67
FT DISULFID 83..163
FT DISULFID 144..157
FT DISULFID 238..259
FT DISULFID 271..280
FT VAR_SEQ 6..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055507"
FT VARIANT 77
FT /note="A -> V (in dbSNP:rs2302466)"
FT /id="VAR_028438"
FT VARIANT 101
FT /note="I -> V (in dbSNP:rs6840615)"
FT /id="VAR_028439"
FT VARIANT 125
FT /note="R -> H (in dbSNP:rs2302465)"
FT /id="VAR_021964"
FT VARIANT 145
FT /note="R -> Q (in dbSNP:rs2302464)"
FT /id="VAR_021965"
FT CONFLICT 36
FT /note="G -> A (in Ref. 1; BAA04885)"
FT /evidence="ECO:0000305"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:1ISI"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1ISI"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1ISI"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1ISI"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1ISI"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1ISI"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:1ISI"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:1ISI"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1ISI"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:1ISI"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:1ISI"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1ISI"
SQ SEQUENCE 318 AA; 35724 MW; E0DD04C89A8F4215 CRC64;
MAAQGCAASR LLQLLLQLLL LLLLLAAGGA RARWRGEGTS AHLRDIFLGR CAEYRALLSP
EQRNKNCTAI WEAFKVALDK DPCSVLPSDY DLFINLSRHS IPRDKSLFWE NSHLLVNSFA
DNTRRFMPLS DVLYGRVADF LSWCRQKNDS GLDYQSCPTS EDCENNPVDS FWKRASIQYS
KDSSGVIHVM LNGSEPTGAY PIKGFFADYE IPNLQKEKIT RIEIWVMHEI GGPNVESCGE
GSMKVLEKRL KDMGFQYSCI NDYRPVKLLQ CVDHSTHPDC ALKSAAAATQ RKAPSLYTEQ
RAGLIIPLFL VLASRTQL
