ASB9_HUMAN
ID ASB9_HUMAN Reviewed; 294 AA.
AC Q96DX5; A8K8A5; Q9BVF5; Q9NWS5; Q9Y4T3;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ankyrin repeat and SOCS box protein 9;
DE Short=ASB-9;
GN Name=ASB9;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Cervix, and Skin;
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 [5]
RP FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20302626; DOI=10.1186/1741-7007-8-23;
RA Kwon S., Kim D., Rhee J.W., Park J.A., Kim D.W., Kim D.S., Lee Y.,
RA Kwon H.J.;
RT "ASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits
RT mitochondrial function.";
RL BMC Biol. 8:23-23(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) (ISOFORM 2), AND FUNCTION.
RX PubMed=22418839; DOI=10.1007/s10930-012-9401-1;
RA Fei X., Gu X., Fan S., Yang Z., Li F., Zhang C., Gong W., Mao Y., Ji C.;
RT "Crystal structure of human ASB9-2 and substrate-recognition of CKB.";
RL Protein J. 31:275-284(2012).
CC -!- FUNCTION: Substrate-recognition component of a SCF-like ECS (Elongin-
CC Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation of
CC target proteins. Recognizes at least two forms of creatine kinase, CKB
CC and CKMT1A. {ECO:0000269|PubMed:22418839}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC Q96DX5; Q08043: ACTN3; NbExp=3; IntAct=EBI-745641, EBI-2880652;
CC Q96DX5; Q8WXK3-2: ASB13; NbExp=3; IntAct=EBI-745641, EBI-12015080;
CC Q96DX5; P12277: CKB; NbExp=10; IntAct=EBI-745641, EBI-357706;
CC Q96DX5; P06732: CKM; NbExp=10; IntAct=EBI-745641, EBI-4287089;
CC Q96DX5; P12532: CKMT1B; NbExp=3; IntAct=EBI-745641, EBI-1050662;
CC Q96DX5; P46108: CRK; NbExp=2; IntAct=EBI-745641, EBI-886;
CC Q96DX5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-745641, EBI-10976677;
CC Q96DX5; Q15369: ELOC; NbExp=3; IntAct=EBI-745641, EBI-301231;
CC Q96DX5; Q9Y3B2: EXOSC1; NbExp=3; IntAct=EBI-745641, EBI-371892;
CC Q96DX5; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-745641, EBI-10226858;
CC Q96DX5; V9HWH2: HEL-S-29; NbExp=3; IntAct=EBI-745641, EBI-10284791;
CC Q96DX5; Q9NWT6: HIF1AN; NbExp=5; IntAct=EBI-745641, EBI-745632;
CC Q96DX5; P54652: HSPA2; NbExp=3; IntAct=EBI-745641, EBI-356991;
CC Q96DX5; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-745641, EBI-1055254;
CC Q96DX5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-745641, EBI-10975473;
CC Q96DX5; P06239-3: LCK; NbExp=3; IntAct=EBI-745641, EBI-13287659;
CC Q96DX5; P02545: LMNA; NbExp=3; IntAct=EBI-745641, EBI-351935;
CC Q96DX5; O60260-5: PRKN; NbExp=3; IntAct=EBI-745641, EBI-21251460;
CC Q96DX5; Q96CP1: RELA; NbExp=3; IntAct=EBI-745641, EBI-10489476;
CC Q96DX5; Q16637: SMN2; NbExp=3; IntAct=EBI-745641, EBI-395421;
CC Q96DX5; Q13148: TARDBP; NbExp=3; IntAct=EBI-745641, EBI-372899;
CC Q96DX5-3; P54253: ATXN1; NbExp=6; IntAct=EBI-25843552, EBI-930964;
CC Q96DX5-3; P46379-2: BAG6; NbExp=3; IntAct=EBI-25843552, EBI-10988864;
CC Q96DX5-3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-25843552, EBI-10976677;
CC Q96DX5-3; O14645: DNALI1; NbExp=3; IntAct=EBI-25843552, EBI-395638;
CC Q96DX5-3; P28799: GRN; NbExp=3; IntAct=EBI-25843552, EBI-747754;
CC Q96DX5-3; O43464: HTRA2; NbExp=3; IntAct=EBI-25843552, EBI-517086;
CC Q96DX5-3; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-25843552, EBI-6398041;
CC Q96DX5-3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25843552, EBI-1055254;
CC Q96DX5-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25843552, EBI-10975473;
CC Q96DX5-3; O14901: KLF11; NbExp=3; IntAct=EBI-25843552, EBI-948266;
CC Q96DX5-3; P35240-4: NF2; NbExp=3; IntAct=EBI-25843552, EBI-1014514;
CC Q96DX5-3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-25843552, EBI-2811583;
CC Q96DX5-3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-25843552, EBI-25882629;
CC Q96DX5-3; O60260-5: PRKN; NbExp=3; IntAct=EBI-25843552, EBI-21251460;
CC Q96DX5-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25843552, EBI-5235340;
CC Q96DX5-3; Q13148: TARDBP; NbExp=3; IntAct=EBI-25843552, EBI-372899;
CC Q96DX5-3; P54577: YARS1; NbExp=3; IntAct=EBI-25843552, EBI-1048893;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20302626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96DX5-1; Sequence=Displayed;
CC Name=2; Synonyms=ASB9deltaSOCS;
CC IsoId=Q96DX5-2; Sequence=VSP_000271;
CC Name=3;
CC IsoId=Q96DX5-3; Sequence=VSP_043158, VSP_000271;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis, kidney, and
CC liver. {ECO:0000269|PubMed:20302626}.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin-protein ligase
CC complexes. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Does not interact with the Elongin BC
CC complex, likely to be a negative regulator of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45706.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK000643; BAA91302.1; -; mRNA.
DR EMBL; AK292270; BAF84959.1; -; mRNA.
DR EMBL; AL080091; CAB45706.2; ALT_INIT; mRNA.
DR EMBL; CH471074; EAW98871.1; -; Genomic_DNA.
DR EMBL; CH471074; EAW98874.1; -; Genomic_DNA.
DR EMBL; BC001244; AAH01244.1; -; mRNA.
DR EMBL; BC013172; AAH13172.1; -; mRNA.
DR CCDS; CCDS14163.1; -. [Q96DX5-2]
DR CCDS; CCDS35208.1; -. [Q96DX5-1]
DR CCDS; CCDS55372.1; -. [Q96DX5-3]
DR RefSeq; NP_001026909.1; NM_001031739.2. [Q96DX5-1]
DR RefSeq; NP_001162002.1; NM_001168530.1. [Q96DX5-3]
DR RefSeq; NP_001162003.1; NM_001168531.1. [Q96DX5-2]
DR RefSeq; NP_076992.1; NM_024087.2. [Q96DX5-2]
DR RefSeq; XP_005274503.1; XM_005274446.1. [Q96DX5-1]
DR PDB; 3D9H; X-ray; 2.20 A; A=1-258.
DR PDB; 3ZKJ; X-ray; 2.58 A; A/D=35-294.
DR PDB; 3ZNG; X-ray; 2.85 A; A/D=35-294.
DR PDB; 6V9H; EM; 4.10 A; C=1-294.
DR PDBsum; 3D9H; -.
DR PDBsum; 3ZKJ; -.
DR PDBsum; 3ZNG; -.
DR PDBsum; 6V9H; -.
DR AlphaFoldDB; Q96DX5; -.
DR SMR; Q96DX5; -.
DR BioGRID; 126615; 44.
DR CORUM; Q96DX5; -.
DR DIP; DIP-52905N; -.
DR IntAct; Q96DX5; 40.
DR MINT; Q96DX5; -.
DR STRING; 9606.ENSP00000369855; -.
DR iPTMnet; Q96DX5; -.
DR PhosphoSitePlus; Q96DX5; -.
DR BioMuta; ASB9; -.
DR DMDM; 29839756; -.
DR REPRODUCTION-2DPAGE; IPI00179183; -.
DR EPD; Q96DX5; -.
DR jPOST; Q96DX5; -.
DR MassIVE; Q96DX5; -.
DR MaxQB; Q96DX5; -.
DR PaxDb; Q96DX5; -.
DR PeptideAtlas; Q96DX5; -.
DR PRIDE; Q96DX5; -.
DR ProteomicsDB; 76334; -. [Q96DX5-1]
DR ProteomicsDB; 76335; -. [Q96DX5-2]
DR ProteomicsDB; 76336; -. [Q96DX5-3]
DR Antibodypedia; 502; 176 antibodies from 28 providers.
DR DNASU; 140462; -.
DR Ensembl; ENST00000380483.7; ENSP00000369850.3; ENSG00000102048.16. [Q96DX5-3]
DR Ensembl; ENST00000380485.7; ENSP00000369852.3; ENSG00000102048.16. [Q96DX5-2]
DR Ensembl; ENST00000380488.9; ENSP00000369855.4; ENSG00000102048.16. [Q96DX5-1]
DR Ensembl; ENST00000546332.1; ENSP00000438943.1; ENSG00000102048.16. [Q96DX5-2]
DR GeneID; 140462; -.
DR KEGG; hsa:140462; -.
DR MANE-Select; ENST00000380488.9; ENSP00000369855.4; NM_001031739.3; NP_001026909.1.
DR UCSC; uc004cwk.4; human. [Q96DX5-1]
DR CTD; 140462; -.
DR GeneCards; ASB9; -.
DR HGNC; HGNC:17184; ASB9.
DR HPA; ENSG00000102048; Group enriched (kidney, liver, lymphoid tissue, pancreas, testis).
DR MIM; 300890; gene.
DR neXtProt; NX_Q96DX5; -.
DR OpenTargets; ENSG00000102048; -.
DR PharmGKB; PA25037; -.
DR VEuPathDB; HostDB:ENSG00000102048; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000157160; -.
DR HOGENOM; CLU_000134_4_0_1; -.
DR InParanoid; Q96DX5; -.
DR OMA; MRDFVSD; -.
DR OrthoDB; 1546307at2759; -.
DR PhylomeDB; Q96DX5; -.
DR TreeFam; TF331945; -.
DR PathwayCommons; Q96DX5; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96DX5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140462; 10 hits in 742 CRISPR screens.
DR EvolutionaryTrace; Q96DX5; -.
DR GenomeRNAi; 140462; -.
DR Pharos; Q96DX5; Tbio.
DR PRO; PR:Q96DX5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96DX5; protein.
DR Bgee; ENSG00000102048; Expressed in islet of Langerhans and 113 other tissues.
DR ExpressionAtlas; Q96DX5; baseline and differential.
DR Genevisible; Q96DX5; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR CDD; cd03728; SOCS_ASB_9_11; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037333; ASB9/11_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..294
FT /note="Ankyrin repeat and SOCS box protein 9"
FT /id="PRO_0000066940"
FT REPEAT 35..64
FT /note="ANK 1"
FT REPEAT 68..97
FT /note="ANK 2"
FT REPEAT 101..130
FT /note="ANK 3"
FT REPEAT 133..162
FT /note="ANK 4"
FT REPEAT 166..195
FT /note="ANK 5"
FT REPEAT 198..227
FT /note="ANK 6"
FT DOMAIN 240..294
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT SITE 103
FT /note="Essential for binding to CKB"
FT SITE 107
FT /note="Essential for binding to CKB"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 145..154
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043158"
FT VAR_SEQ 255..294
FT /note="PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL -> ASLPKPKP
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_000271"
FT CONFLICT 192
FT /note="D -> V (in Ref. 2; CAB45706)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="E -> G (in Ref. 2; CAB45706)"
FT /evidence="ECO:0000305"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3D9H"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:3D9H"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:3D9H"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:3ZKJ"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:3ZKJ"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3ZKJ"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:3ZKJ"
SQ SEQUENCE 294 AA; 31858 MW; A1784DCFC294D85A CRC64;
MDGKQGGMDG SKPAGPRDFP GIRLLSNPLM GDAVSDWSPM HEAAIHGHQL SLRNLISQGW
AVNIITADHV SPLHEACLGG HLSCVKILLK HGAQVNGVTA DWHTPLFNAC VSGSWDCVNL
LLQHGASVQP ESDLASPIHE AARRGHVECV NSLIAYGGNI DHKISHLGTP LYLACENQQR
ACVKKLLESG ADVNQGKGQD SPLHAVARTA SEELACLLMD FGADTQAKNA EGKRPVELVP
PESPLAQLFL EREGPPSLMQ LCRLRIRKCF GIQQHHKITK LVLPEDLKQF LLHL
