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AHRR_HUMAN
ID   AHRR_HUMAN              Reviewed;         701 AA.
AC   A9YTQ3; A7MBN5; D6RAZ1; Q9HAZ3; Q9ULI6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Aryl hydrocarbon receptor repressor;
DE            Short=AhR repressor;
DE            Short=AhRR;
DE   AltName: Full=Class E basic helix-loop-helix protein 77;
DE            Short=bHLHe77;
GN   Name=AHRR; Synonyms=BHLHE77, KIAA1234;
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] (ISOFORM 3), TISSUE SPECIFICITY, AND
RP   VARIANT PRO-114.
RX   PubMed=11835227; DOI=10.1002/tera.1093;
RA   Fujita H., Kosaki R., Yoshihashi H., Ogata T., Tomita M., Hasegawa T.,
RA   Takahashi T., Matsuo N., Kosaki K.;
RT   "Characterization of the aryl hydrocarbon receptor repressor gene and
RT   association of its Pro185Ala polymorphism with micropenis.";
RL   Teratology 65:10-18(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-189.
RA   Karchner S.I., Evans B., Jenny M.J., Hahn M.E.;
RT   "Identification and functional analysis of a human AHR repressor.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-189.
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-189.
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-189.
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   [7]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14672759; DOI=10.1016/j.lfs.2003.07.022;
RA   Yamamoto J., Ihara K., Nakayama H., Hikino S., Satoh K., Kubo N., Iida T.,
RA   Fujii Y., Hara T.;
RT   "Characteristic expression of aryl hydrocarbon receptor repressor gene in
RT   human tissues: organ-specific distribution and variable induction patterns
RT   in mononuclear cells.";
RL   Life Sci. 74:1039-1049(2004).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17980155; DOI=10.1016/j.bbrc.2007.10.140;
RA   Kanno Y., Miyama Y., Takane Y., Nakahama T., Inouye Y.;
RT   "Identification of intracellular localization signals and of mechanisms
RT   underlining the nucleocytoplasmic shuttling of human aryl hydrocarbon
RT   receptor repressor.";
RL   Biochem. Biophys. Res. Commun. 364:1026-1031(2007).
RN   [9]
RP   FUNCTION.
RX   PubMed=17890447; DOI=10.1124/dmd.107.016253;
RA   Haarmann-Stemmann T., Bothe H., Kohli A., Sydlik U., Abel J., Fritsche E.;
RT   "Analysis of the transcriptional regulation and molecular function of the
RT   aryl hydrocarbon receptor repressor in human cell lines.";
RL   Drug Metab. Dispos. 35:2262-2269(2007).
RN   [10]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=18172554; DOI=10.1172/jci30024;
RA   Zudaire E., Cuesta N., Murty V., Woodson K., Adams L., Gonzalez N.,
RA   Martinez A., Narayan G., Kirsch I., Franklin W., Hirsch F., Birrer M.,
RA   Cuttitta F.;
RT   "The aryl hydrocarbon receptor repressor is a putative tumor suppressor
RT   gene in multiple human cancers.";
RL   J. Clin. Invest. 118:640-650(2008).
RN   [11]
RP   POLYMORPHISM, AND ASSOCIATION WITH SUSCEPTIBILITY TO MALE INFERTILITY.
RX   PubMed=15474075; DOI=10.1016/j.fertnstert.2004.06.027;
RA   Watanabe M., Sueoka K., Sasagawa I., Nakabayashi A., Yoshimura Y.,
RA   Ogata T.;
RT   "Association of male infertility with Pro185Ala polymorphism in the aryl
RT   hydrocarbon receptor repressor gene: implication for the susceptibility to
RT   dioxins.";
RL   Fertil. Steril. 82:1067-1071(2004).
RN   [12]
RP   POLYMORPHISM, AND ASSOCIATION WITH SUSCEPTIBILITY TO ENDOMETRIOSIS.
RX   PubMed=16084889; DOI=10.1016/j.fertnstert.2005.01.130;
RA   Tsuchiya M., Katoh T., Motoyama H., Sasaki H., Tsugane S., Ikenoue T.;
RT   "Analysis of the AhR, ARNT, and AhRR gene polymorphisms: genetic
RT   contribution to endometriosis susceptibility and severity.";
RL   Fertil. Steril. 84:454-458(2005).
RN   [13]
RP   POLYMORPHISM, AND ASSOCIATION WITH SUSCEPTIBILITY TO MALE INFERTILITY.
RX   PubMed=17559847; DOI=10.1016/j.fertnstert.2006.12.041;
RA   Merisalu A., Punab M., Altmaee S., Haller K., Tiido T., Peters M.,
RA   Salumets A.;
RT   "The contribution of genetic variations of aryl hydrocarbon receptor
RT   pathway genes to male factor infertility.";
RL   Fertil. Steril. 88:854-859(2007).
RN   [14]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-577 AND LYS-660, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-577 AND LYS-660, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [16] {ECO:0007744|PDB:5Y7Y}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 27-280 IN COMPLEX WITH ARNT, AND
RP   INTERACTION WITH ARNT.
RX   PubMed=28904176; DOI=10.1074/jbc.m117.812974;
RA   Sakurai S., Shimizu T., Ohto U.;
RT   "The crystal structure of the AhRR-ARNT heterodimer reveals the structural
RT   basis of the repression of AhR-mediated transcription.";
RL   J. Biol. Chem. 292:17609-17616(2017).
CC   -!- FUNCTION: Mediates dioxin toxicity and is involved in regulation of
CC       cell growth and differentiation. Represses the transcription activity
CC       of AHR by competing with this transcription factor for heterodimer
CC       formation with the ARNT and subsequently binding to the xenobiotic
CC       response element (XRE) sequence present in the promoter regulatory
CC       region of variety of genes. Represses CYP1A1 by binding the XRE
CC       sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its
CC       expression by associating with its own XRE site.
CC       {ECO:0000269|PubMed:17890447, ECO:0000269|PubMed:18172554}.
CC   -!- SUBUNIT: Interacts with ANKRA2, HDAC4 and HDAC5. Interacts with ARNT;
CC       forms a heterodimer with ARNT (PubMed:28904176). {ECO:0000250,
CC       ECO:0000269|PubMed:28904176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17980155}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17980155}.
CC       Note=Predominantly in the nuclear compartment. First cytoplasmic,
CC       translocates into the nuclear compartment upon interaction with ARNT in
CC       the cytoplasmic compartment.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A9YTQ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A9YTQ3-2; Sequence=VSP_033564;
CC       Name=3;
CC         IsoId=A9YTQ3-3; Sequence=VSP_033563, VSP_033564;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis, lung, ovary, spleen and
CC       pancreas. Highly expressed in mononuclear cells (MNCs) from umbilical
CC       cord blood. Isoform 3 is highly expressed in lung, kidney, spleen and
CC       thymus. Down-regulated malignant tissue from different anatomical
CC       origins, including colon, breast, lung, stomach, cervix, and ovary.
CC       {ECO:0000269|PubMed:11835227, ECO:0000269|PubMed:14672759,
CC       ECO:0000269|PubMed:18172554}.
CC   -!- INDUCTION: By 3-methylcholanthrene (3-MC) in MNCs from adults. By the
CC       heterodimer AHR/ARNT. {ECO:0000269|PubMed:14672759}.
CC   -!- POLYMORPHISM: The Ala-189 allele may be a susceptibility factor for
CC       dioxin-related male infertility. Homozygosity for Ala-189 is observed
CC       in azoospermic individuals at higher frequency than in normozoospermic
CC       individuals (PubMed:15474075, PubMed:17559847). Might also be
CC       associated with susceptibility to and severity of endometriosis.
CC       {ECO:0000269|PubMed:15474075, ECO:0000269|PubMed:17559847}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABX89616.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA86548.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF293639; AAG33381.1; -; Genomic_DNA.
DR   EMBL; AF293629; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293630; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293631; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293632; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293633; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293634; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293635; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293636; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293637; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; AF293638; AAG33381.1; JOINED; Genomic_DNA.
DR   EMBL; EU293605; ABX89616.1; ALT_INIT; mRNA.
DR   EMBL; AB033060; BAA86548.1; ALT_INIT; mRNA.
DR   EMBL; AC010442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471235; EAW50992.1; -; Genomic_DNA.
DR   EMBL; BC151852; AAI51853.1; -; mRNA.
DR   EMBL; BC152406; AAI52407.1; -; mRNA.
DR   RefSeq; NP_001229341.1; NM_001242412.1.
DR   RefSeq; NP_065782.2; NM_020731.4.
DR   PDB; 5Y7Y; X-ray; 2.40 A; A=27-280.
DR   PDBsum; 5Y7Y; -.
DR   AlphaFoldDB; A9YTQ3; -.
DR   SMR; A9YTQ3; -.
DR   BioGRID; 121558; 7.
DR   STRING; 9606.ENSP00000323816; -.
DR   iPTMnet; A9YTQ3; -.
DR   PhosphoSitePlus; A9YTQ3; -.
DR   BioMuta; AHRR; -.
DR   MassIVE; A9YTQ3; -.
DR   PaxDb; A9YTQ3; -.
DR   PeptideAtlas; A9YTQ3; -.
DR   PRIDE; A9YTQ3; -.
DR   ProteomicsDB; 2518; -. [A9YTQ3-1]
DR   ProteomicsDB; 2519; -. [A9YTQ3-2]
DR   ProteomicsDB; 2520; -. [A9YTQ3-3]
DR   Antibodypedia; 8774; 125 antibodies from 18 providers.
DR   DNASU; 57491; -.
DR   GeneID; 57491; -.
DR   UCSC; uc003jav.4; human. [A9YTQ3-1]
DR   CTD; 57491; -.
DR   DisGeNET; 57491; -.
DR   GeneCards; AHRR; -.
DR   HGNC; HGNC:346; AHRR.
DR   HPA; ENSG00000063438; Tissue enriched (testis).
DR   MIM; 606517; gene.
DR   neXtProt; NX_A9YTQ3; -.
DR   PharmGKB; PA24639; -.
DR   VEuPathDB; HostDB:ENSG00000063438; -.
DR   VEuPathDB; HostDB:ENSG00000288622; -.
DR   eggNOG; KOG3560; Eukaryota.
DR   HOGENOM; CLU_023661_0_0_1; -.
DR   InParanoid; A9YTQ3; -.
DR   OrthoDB; 325707at2759; -.
DR   PhylomeDB; A9YTQ3; -.
DR   TreeFam; TF352074; -.
DR   PathwayCommons; A9YTQ3; -.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR   Reactome; R-HSA-211976; Endogenous sterols.
DR   Reactome; R-HSA-211981; Xenobiotics.
DR   Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
DR   SignaLink; A9YTQ3; -.
DR   BioGRID-ORCS; 57491; 12 hits in 1092 CRISPR screens.
DR   ChiTaRS; AHRR; human.
DR   GenomeRNAi; 57491; -.
DR   Pharos; A9YTQ3; Tbio.
DR   PRO; PR:A9YTQ3; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; A9YTQ3; protein.
DR   ExpressionAtlas; A9YTQ3; baseline and differential.
DR   Genevisible; A9YTQ3; HS.
DR   GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR039091; AHR/AHRR.
DR   InterPro; IPR039092; AHRR.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   PANTHER; PTHR10649; PTHR10649; 1.
DR   PANTHER; PTHR10649:SF3; PTHR10649:SF3; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF00989; PAS; 1.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; DNA-binding;
KW   Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..701
FT                   /note="Aryl hydrocarbon receptor repressor"
FT                   /id="PRO_0000333857"
FT   DOMAIN          28..81
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          112..182
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..701
FT                   /note="Needed for transcriptional repression"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        371..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        577
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        660
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..4
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_033563"
FT   VAR_SEQ         240
FT                   /note="L -> LARGSQAWQLRLCCPEPLM (in isoform 2 and isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:10574462,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033564"
FT   VARIANT         114
FT                   /note="L -> P (in dbSNP:rs35008248)"
FT                   /evidence="ECO:0000269|PubMed:11835227"
FT                   /id="VAR_043308"
FT   VARIANT         189
FT                   /note="P -> A (in dbSNP:rs2292596)"
FT                   /evidence="ECO:0000269|PubMed:10574462,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.5"
FT                   /id="VAR_043309"
FT   VARIANT         373
FT                   /note="G -> V (in dbSNP:rs2303738)"
FT                   /id="VAR_043310"
FT   VARIANT         627
FT                   /note="D -> H (in dbSNP:rs34453673)"
FT                   /id="VAR_043311"
FT   HELIX           39..53
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           67..89
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           117..122
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   STRAND          123..130
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           143..147
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           159..162
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           168..175
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           197..206
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   STRAND          221..230
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   STRAND          235..250
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
FT   STRAND          268..276
FT                   /evidence="ECO:0007829|PDB:5Y7Y"
SQ   SEQUENCE   701 AA;  76265 MW;  488F6D41298760E0 CRC64;
     MPRTMIPPGE CTYAGRKRRR PLQKQRPAVG AEKSNPSKRH RDRLNAELDH LASLLPFPPD
     IISKLDKLSV LRLSVSYLRV KSFFQVVQEQ SSRQPAAGAP SPGDSCPLAG SAVLEGRLLL
     ESLNGFALVV SAEGTIFYAS ATIVDYLGFH QTDVMHQNIY DYIHVDDRQD FCRQLHWAMD
     PPQVVFGQPP PLETGDDAIL GRLLRAQEWG TGTPTEYSAF LTRCFICRVR CLLDSTSGFL
     TMQFQGKLKF LFGQKKKAPS GAMLPPRLSL FCIAAPVLLP SAAEMKMRSA LLRAKPRADT
     AATADAKVKA TTSLCESELH GKPNYSAGRS SRESGVLVLR EQTDAGRWAQ VPARAPCLCL
     RGGPDLVLDP KGGSGDREEE QHRMLSRASG VTGRRETPGP TKPLPWTAGK HSEDGARPRL
     QPSKNDPPSL RPMPRGSCLP CPCVQGTFRN SPISHPPSPS PSAYSSRTSR PMRDVGEDQV
     HPPLCHFPQR SLQHQLPQPG AQRFATRGYP MEDMKLQGVP MPPGDLCGPT LLLDVSIKME
     KDSGCEGAAD GCVPSQVWLG ASDRSHPATF PTRMHLKTEP DSRQQVYISH LGHGVRGAQP
     HGRATAGRSR ELTPFHPAHC ACLEPTDGLP QSEPPHQLCA RGRGEQSCTC RAAEAAPVVK
     REPLDSPQWA THSQGMVPGM LPKSALATLV PPQASGCTFL P
 
 
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