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   24-JAN-2024, entry version 184.
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.
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   EMDB; EMD-21120; -.
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; 9606-ENSP00000369855; -.
DR   PeptideAtlas; Q96DX5; -.
DR   ProteomicsDB; 76334; -. [Q96DX5-1]
DR   ProteomicsDB; 76335; -. [Q96DX5-2]
DR   ProteomicsDB; 76336; -. [Q96DX5-3]
DR   Pumba; Q96DX5; -.
DR   Antibodypedia; 502; 196 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   AGR; HGNC:17184; -.
DR   CTD; 140462; -.
DR   GeneCards; ASB9; -.
DR   HGNC; HGNC:17184; ASB9.
DR   HPA; ENSG00000102048; Tissue enhanced (kidney, liver, 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; QHHKITG; -.
DR   OrthoDB; 50291at2759; -.
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   SIGNOR; Q96DX5; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 140462; 10 hits in 813 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 male germ line stem cell (sensu Vertebrata) in testis and 115 other cell types or tissues.
DR   ExpressionAtlas; Q96DX5; baseline and differential.
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; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.750.20; SOCS box; 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   PANTHER; PTHR24136:SF17; ANKYRIN REPEAT AND SOCS BOX PROTEIN 9; 1.
DR   PANTHER; PTHR24136; SOWAH (DROSOPHILA) HOMOLOG; 1.
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; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF158235; SOCS box-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50225; SOCS; 1.
DR   Genevisible; Q96DX5; HS.
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
//