MYNN_HUMAN
ID MYNN_HUMAN Reviewed; 610 AA.
AC Q9NPC7; B2R6C9; Q6QHA6; Q6QHA7; Q6R3G1; Q6R3G2; Q6R4A0; Q7Z716; Q7Z717;
AC Q86Z11; Q86Z12; Q9NS01; Q9UIW8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Myoneurin;
DE AltName: Full=Zinc finger and BTB domain-containing protein 31;
GN Name=MYNN; Synonyms=OSZF, ZBTB31; ORFNames=SBBIZ1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 264-610 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 32-610
RP (ISOFORM 4), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10873615; DOI=10.1006/bbrc.2000.2862;
RA Alliel P.M., Seddiqi N., Goudou D., Cifuentes-Diaz C., Romero N.,
RA Velasco E., Rieger F., Perin J.-P.;
RT "Myoneurin, a novel member of the BTB/POZ-zinc finger family highly
RT expressed in human muscle.";
RL Biochem. Biophys. Res. Commun. 273:385-391(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RA Ito S., Naito N., Ouchida M., Shimizu K.;
RT "Cloning and characterization of a novel human gene, OSZF, encoding a zinc
RT finger protein with BTB/POZ domain.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Dendritic cell;
RA Zhang W., Wan T., Yuan Z., Cao X.;
RT "A zinc finger protein SBBIZ1 expressed in human dendritic cells.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo, and 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 MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14694499; DOI=10.1002/mus.10526;
RA Cifuentes-Diaz C., Bitoun M., Goudou D., Seddiqi N., Romero N., Rieger F.,
RA Perin J.-P., Alliel P.M.;
RT "Neuromuscular expression of the BTB/POZ and zinc finger protein
RT myoneurin.";
RL Muscle Nerve 29:59-65(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-117.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the BTB domain of human myoneurin.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- INTERACTION:
CC Q9NPC7; Q92688: ANP32B; NbExp=3; IntAct=EBI-3446748, EBI-762428;
CC Q9NPC7; P27797: CALR; NbExp=3; IntAct=EBI-3446748, EBI-1049597;
CC Q9NPC7; P12830: CDH1; NbExp=3; IntAct=EBI-3446748, EBI-727477;
CC Q9NPC7; Q15078: CDK5R1; NbExp=3; IntAct=EBI-3446748, EBI-746189;
CC Q9NPC7; P36957: DLST; NbExp=3; IntAct=EBI-3446748, EBI-351007;
CC Q9NPC7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-3446748, EBI-10976677;
CC Q9NPC7; Q9BRP7: FDXACB1; NbExp=3; IntAct=EBI-3446748, EBI-10297077;
CC Q9NPC7; P28799: GRN; NbExp=3; IntAct=EBI-3446748, EBI-747754;
CC Q9NPC7; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-3446748, EBI-1055254;
CC Q9NPC7; O60333-2: KIF1B; NbExp=3; IntAct=EBI-3446748, EBI-10975473;
CC Q9NPC7; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-3446748, EBI-1055945;
CC Q9NPC7; O60260-5: PRKN; NbExp=3; IntAct=EBI-3446748, EBI-21251460;
CC Q9NPC7; P50454: SERPINH1; NbExp=3; IntAct=EBI-3446748, EBI-350723;
CC Q9NPC7; P37173: TGFBR2; NbExp=3; IntAct=EBI-3446748, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14694499}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NPC7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPC7-2; Sequence=VSP_020216;
CC Name=3;
CC IsoId=Q9NPC7-3; Sequence=VSP_020215, VSP_020217;
CC Name=4; Synonyms=m4b;
CC IsoId=Q9NPC7-4; Sequence=VSP_020213, VSP_020214;
CC -!- TISSUE SPECIFICITY: Mainly expressed in the neuromuscular system.
CC Located in and around synaptic myonuclei in adult muscle. Expression is
CC dysregulated after nerve injury. Also found in the testis, ovary and
CC placenta. {ECO:0000269|PubMed:10873615, ECO:0000269|PubMed:14694499}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF148848; AAF73138.1; -; mRNA.
DR EMBL; AY286322; AAP44763.1; -; Genomic_DNA.
DR EMBL; AY286321; AAP44763.1; JOINED; Genomic_DNA.
DR EMBL; AY286328; AAP44764.1; -; Genomic_DNA.
DR EMBL; AY286323; AAP44764.1; JOINED; Genomic_DNA.
DR EMBL; AY286325; AAP44764.1; JOINED; Genomic_DNA.
DR EMBL; AY286324; AAP44764.1; JOINED; Genomic_DNA.
DR EMBL; AY286326; AAP44764.1; JOINED; Genomic_DNA.
DR EMBL; AY286327; AAP44764.1; JOINED; Genomic_DNA.
DR EMBL; AY514901; AAR99055.1; -; mRNA.
DR EMBL; AY515294; AAR99843.1; -; Genomic_DNA.
DR EMBL; AY515691; AAS38566.1; -; mRNA.
DR EMBL; AY515692; AAS38567.1; -; mRNA.
DR EMBL; AY541760; AAS87376.1; -; mRNA.
DR EMBL; AY541761; AAS87377.1; -; mRNA.
DR EMBL; AB079777; BAC55898.1; -; mRNA.
DR EMBL; AB079778; BAC55899.1; -; mRNA.
DR EMBL; AB079779; BAC55900.1; -; Genomic_DNA.
DR EMBL; AF076249; AAF80160.1; -; mRNA.
DR EMBL; AF155508; AAF74822.1; -; mRNA.
DR EMBL; AK021646; BAB13862.1; -; mRNA.
DR EMBL; AK092022; BAG52468.1; -; mRNA.
DR EMBL; AK312527; BAG35426.1; -; mRNA.
DR EMBL; AL133070; CAB61393.1; -; mRNA.
DR EMBL; BX648128; CAI46035.1; -; mRNA.
DR EMBL; CH471052; EAW78544.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78546.1; -; Genomic_DNA.
DR EMBL; BC033620; AAH33620.1; -; mRNA.
DR CCDS; CCDS3207.1; -. [Q9NPC7-1]
DR CCDS; CCDS54671.1; -. [Q9NPC7-2]
DR PIR; JC7315; JC7315.
DR PIR; T42670; T42670.
DR RefSeq; NP_001172047.1; NM_001185118.1. [Q9NPC7-1]
DR RefSeq; NP_001172048.1; NM_001185119.1. [Q9NPC7-2]
DR RefSeq; NP_061127.1; NM_018657.4. [Q9NPC7-1]
DR RefSeq; XP_011511289.1; XM_011512987.1.
DR RefSeq; XP_016862353.1; XM_017006864.1.
DR PDB; 2VPK; X-ray; 2.00 A; A=4-117.
DR PDBsum; 2VPK; -.
DR AlphaFoldDB; Q9NPC7; -.
DR SMR; Q9NPC7; -.
DR BioGRID; 120982; 11.
DR IntAct; Q9NPC7; 19.
DR STRING; 9606.ENSP00000326240; -.
DR iPTMnet; Q9NPC7; -.
DR PhosphoSitePlus; Q9NPC7; -.
DR BioMuta; MYNN; -.
DR DMDM; 74761639; -.
DR EPD; Q9NPC7; -.
DR jPOST; Q9NPC7; -.
DR MassIVE; Q9NPC7; -.
DR MaxQB; Q9NPC7; -.
DR PaxDb; Q9NPC7; -.
DR PeptideAtlas; Q9NPC7; -.
DR PRIDE; Q9NPC7; -.
DR ProteomicsDB; 81968; -. [Q9NPC7-1]
DR ProteomicsDB; 81969; -. [Q9NPC7-2]
DR ProteomicsDB; 81970; -. [Q9NPC7-3]
DR ProteomicsDB; 81971; -. [Q9NPC7-4]
DR Antibodypedia; 18640; 254 antibodies from 26 providers.
DR DNASU; 55892; -.
DR Ensembl; ENST00000349841.10; ENSP00000326240.4; ENSG00000085274.16. [Q9NPC7-1]
DR Ensembl; ENST00000356716.8; ENSP00000349150.3; ENSG00000085274.16. [Q9NPC7-1]
DR Ensembl; ENST00000544106.5; ENSP00000440637.1; ENSG00000085274.16. [Q9NPC7-2]
DR Ensembl; ENST00000602751.5; ENSP00000473654.1; ENSG00000085274.16. [Q9NPC7-4]
DR GeneID; 55892; -.
DR KEGG; hsa:55892; -.
DR MANE-Select; ENST00000349841.10; ENSP00000326240.4; NM_018657.5; NP_061127.1.
DR UCSC; uc003fft.4; human. [Q9NPC7-1]
DR CTD; 55892; -.
DR DisGeNET; 55892; -.
DR GeneCards; MYNN; -.
DR HGNC; HGNC:14955; MYNN.
DR HPA; ENSG00000085274; Low tissue specificity.
DR MIM; 606042; gene.
DR neXtProt; NX_Q9NPC7; -.
DR OpenTargets; ENSG00000085274; -.
DR PharmGKB; PA31393; -.
DR VEuPathDB; HostDB:ENSG00000085274; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161266; -.
DR HOGENOM; CLU_022540_1_0_1; -.
DR InParanoid; Q9NPC7; -.
DR OMA; TNCDAKF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9NPC7; -.
DR TreeFam; TF330787; -.
DR PathwayCommons; Q9NPC7; -.
DR SignaLink; Q9NPC7; -.
DR BioGRID-ORCS; 55892; 11 hits in 1143 CRISPR screens.
DR ChiTaRS; MYNN; human.
DR EvolutionaryTrace; Q9NPC7; -.
DR GenomeRNAi; 55892; -.
DR Pharos; Q9NPC7; Tbio.
DR PRO; PR:Q9NPC7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NPC7; protein.
DR Bgee; ENSG00000085274; Expressed in buccal mucosa cell and 195 other tissues.
DR ExpressionAtlas; Q9NPC7; baseline and differential.
DR Genevisible; Q9NPC7; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..610
FT /note="Myoneurin"
FT /id="PRO_0000248217"
FT DOMAIN 24..89
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 302..324
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 330..352
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..381
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 387..409
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 415..437
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 443..465
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 471..493
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 499..522
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 169..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..190
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 257..262
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 523..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 89..91
FT /note="SWN -> RDI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10873615, ECO:0000303|Ref.3"
FT /id="VSP_020213"
FT VAR_SEQ 92..610
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10873615, ECO:0000303|Ref.3"
FT /id="VSP_020214"
FT VAR_SEQ 495..500
FT /note="GERPFI -> VVWSMN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10873615"
FT /id="VSP_020215"
FT VAR_SEQ 496..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_020216"
FT VAR_SEQ 501..610
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10873615"
FT /id="VSP_020217"
FT CONFLICT 198
FT /note="Q -> R (in Ref. 2; BAC55898/BAC55899)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="E -> D (in Ref. 5; CAB61393)"
FT /evidence="ECO:0000305"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:2VPK"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2VPK"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2VPK"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:2VPK"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:2VPK"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2VPK"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:2VPK"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2VPK"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:2VPK"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2VPK"
SQ SEQUENCE 610 AA; 68682 MW; 842B62DDC2C81480 CRC64;
MQYSHHCEHL LERLNKQREA GFLCDCTIVI GEFQFKAHRN VLASFSEYFG AIYRSTSENN
VFLDQSQVKA DGFQKLLEFI YTGTLNLDSW NVKEIHQAAD YLKVEEVVTK CKIKMEDFAF
IANPSSTEIS SITGNIELNQ QTCLLTLRDY NNREKSEVST DLIQANPKQG ALAKKSSQTK
KKKKAFNSPK TGQNKTVQYP SDILENASVE LFLDANKLPT PVVEQVAQIN DNSELELTSV
VENTFPAQDI VHTVTVKRKR GKSQPNCALK EHSMSNIASV KSPYEAENSG EELDQRYSKA
KPMCNTCGKV FSEASSLRRH MRIHKGVKPY VCHLCGKAFT QCNQLKTHVR THTGEKPYKC
ELCDKGFAQK CQLVFHSRMH HGEEKPYKCD VCNLQFATSS NLKIHARKHS GEKPYVCDRC
GQRFAQASTL TYHVRRHTGE KPYVCDTCGK AFAVSSSLIT HSRKHTGEKP YICGICGKSF
ISSGELNKHF RSHTGERPFI CELCGNSYTD IKNLKKHKTK VHSGADKTLD SSAEDHTLSE
QDSIQKSPLS ETMDVKPSDM TLPLALPLGT EDHHMLLPVT DTQSPTSDTL LRSTVNGYSE
PQLIFLQQLY
