TSH3_HUMAN
ID TSH3_HUMAN Reviewed; 1081 AA.
AC Q63HK5; A1L0U7; Q9H0G6; Q9P254;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Teashirt homolog 3;
DE AltName: Full=Zinc finger protein 537;
GN Name=TSHZ3; Synonyms=KIAA1474, TSH3, ZNF537;
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], AND VARIANT GLY-469.
RC TISSUE=Endometrial tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1081.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-1081.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-1081.
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 TISSUE SPECIFICITY.
RX PubMed=18776146; DOI=10.1242/dev.022442;
RA Caubit X., Lye C.M., Martin E., Core N., Long D.A., Vola C., Jenkins D.,
RA Garratt A.N., Skaer H., Woolf A.S., Fasano L.;
RT "Teashirt 3 is necessary for ureteral smooth muscle differentiation
RT downstream of SHH and BMP4.";
RL Development 135:3301-3310(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP FUNCTION, INTERACTION WITH APBB1; HDAC1 AND HDAC2, IDENTIFICATION IN A
RP TRIMERIC COMPLEX WITH APBB1 AND HDAC1, CHROMATIN-BINDING, MUTAGENESIS OF
RP 953-VAL--TYR-955, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN NEURODEVELOPMENTAL DISORDER.
RX PubMed=27668656; DOI=10.1038/ng.3681;
RA Caubit X., Gubellini P., Andrieux J., Roubertoux P.L., Metwaly M., Jacq B.,
RA Fatmi A., Had-Aissouni L., Kwan K.Y., Salin P., Carlier M., Lieden A.,
RA Rudd E., Shinawi M., Vincent-Delorme C., Cuisset J.M., Lemaitre M.P.,
RA Abderrehamane F., Duban B., Lemaitre J.F., Woolf A.S., Bockenhauer D.,
RA Severac D., Dubois E., Zhu Y., Sestan N., Garratt A.N.,
RA Kerkerian-Le Goff L., Fasano L.;
RT "TSHZ3 deletion causes an autism syndrome and defects in cortical
RT projection neurons.";
RL Nat. Genet. 48:1359-1369(2016).
RN [11]
RP VARIANT GLY-469, AND DEVELOPMENTAL STAGE.
RX PubMed=19745106; DOI=10.1093/ndt/gfp453;
RA Jenkins D., Caubit X., Dimovski A., Matevska N., Lye C.M., Cabuk F.,
RA Gucev Z., Tasic V., Fasano L., Woolf A.S.;
RT "Analysis of TSHZ2 and TSHZ3 genes in congenital pelvi-ureteric junction
RT obstruction.";
RL Nephrol. Dial. Transplant. 25:54-60(2010).
RN [12]
RP STRUCTURE BY NMR OF 200-303.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and the second ZF-C2H2-like domains of
RT human teashirt homolog 3.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Transcriptional regulator involved in developmental
CC processes. Functions in association with APBB1, SET and HDAC factors as
CC a transcriptional repressor, that inhibits the expression of CASP4.
CC TSHZ3-mediated transcription repression involves the recruitment of
CC histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a
CC region surrounding the CASP4 transcriptional start site(s)
CC (PubMed:19343227). Regulates the development of neurons involved in
CC both respiratory rhythm and airflow control. Promotes maintenance of
CC nucleus ambiguus (nA) motoneurons, which govern upper airway function,
CC and establishes a respiratory rhythm generator (RRG) activity
CC compatible with survival at birth. Involved in the differentiation of
CC the proximal uretic smooth muscle cells during developmental processes.
CC Involved in the up-regulation of myocardin, that directs the expression
CC of smooth muscle cells in the proximal ureter (By similarity). Involved
CC in the modulation of glutamatergic synaptic transmission and long-term
CC synaptic potentiation (By similarity). {ECO:0000250|UniProtKB:Q8CGV9,
CC ECO:0000269|PubMed:19343227}.
CC -!- SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID domain 1).
CC Interacts (via N-terminus) with HDAC1 and HDAC2; the interaction is
CC direct. Found in a trimeric complex with APBB1 and HDAC1; the
CC interaction between HDAC1 and APBB1 is mediated by TSHZ3.
CC {ECO:0000269|PubMed:19343227}.
CC -!- INTERACTION:
CC Q63HK5; Q9H9E1: ANKRA2; NbExp=4; IntAct=EBI-9053916, EBI-10215533;
CC Q63HK5; Q9UBZ4: APEX2; NbExp=3; IntAct=EBI-9053916, EBI-742588;
CC Q63HK5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-9053916, EBI-10175300;
CC Q63HK5; Q96MT8: CEP63; NbExp=3; IntAct=EBI-9053916, EBI-741977;
CC Q63HK5; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-9053916, EBI-739624;
CC Q63HK5; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-9053916, EBI-3866319;
CC Q63HK5; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-9053916, EBI-10171858;
CC Q63HK5; P56545-3: CTBP2; NbExp=6; IntAct=EBI-9053916, EBI-10171902;
CC Q63HK5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-9053916, EBI-618309;
CC Q63HK5; O75031: HSF2BP; NbExp=3; IntAct=EBI-9053916, EBI-7116203;
CC Q63HK5; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-9053916, EBI-749265;
CC Q63HK5; Q15323: KRT31; NbExp=3; IntAct=EBI-9053916, EBI-948001;
CC Q63HK5; Q6A162: KRT40; NbExp=3; IntAct=EBI-9053916, EBI-10171697;
CC Q63HK5; Q5JTD7: LRRC73; NbExp=3; IntAct=EBI-9053916, EBI-12003882;
CC Q63HK5; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-9053916, EBI-742610;
CC Q63HK5; Q13084: MRPL28; NbExp=3; IntAct=EBI-9053916, EBI-723426;
CC Q63HK5; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-9053916, EBI-742948;
CC Q63HK5; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-9053916, EBI-11522433;
CC Q63HK5; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-9053916, EBI-14066006;
CC Q63HK5; Q6NUQ1: RINT1; NbExp=5; IntAct=EBI-9053916, EBI-726876;
CC Q63HK5; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-9053916, EBI-1378139;
CC Q63HK5; Q96R06: SPAG5; NbExp=3; IntAct=EBI-9053916, EBI-413317;
CC Q63HK5; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-9053916, EBI-529518;
CC Q63HK5; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-9053916, EBI-11139477;
CC Q63HK5; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-9053916, EBI-1105213;
CC Q63HK5; Q12933: TRAF2; NbExp=3; IntAct=EBI-9053916, EBI-355744;
CC Q63HK5; P36406: TRIM23; NbExp=3; IntAct=EBI-9053916, EBI-740098;
CC Q63HK5; P14373: TRIM27; NbExp=3; IntAct=EBI-9053916, EBI-719493;
CC Q63HK5; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-9053916, EBI-2130429;
CC Q63HK5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-9053916, EBI-12806590;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:19343227}. Cell projection, growth cone
CC {ECO:0000250}. Note=Colocalizes with APBB1 in axonal growth cone (By
CC similarity). Colocalizes with APBB1 in the nucleus. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain; strongly reduced in post-mortem
CC elderly subjects with Alzheimer disease (PubMed:18776146,
CC PubMed:19343227). Expressed in the fetal neocortex (PubMed:27668656).
CC {ECO:0000269|PubMed:18776146, ECO:0000269|PubMed:19343227,
CC ECO:0000269|PubMed:27668656}.
CC -!- DEVELOPMENTAL STAGE: Expressed in peri-urothelial cells of the proximal
CC ureter and renal pelvis at 9 weeks of gestation.
CC {ECO:0000269|PubMed:19745106}.
CC -!- DISEASE: Note=TSHZ3 haploinsufficiency due to proximal chromosome
CC 19q13.11 deletions causes a neurodevelopmental disorder characterized
CC by developmental delay, absent or delayed speech, intellectual
CC disability, and autistic features. Some patients may have reanal tract
CC abnormalities. {ECO:0000269|PubMed:27668656}.
CC -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI27096.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI27097.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66739.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life's first breath - Issue
CC 122 of October 2010;
CC URL="https://web.expasy.org/spotlight/back_issues/122";
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DR EMBL; BX648745; CAH56184.1; -; mRNA.
DR EMBL; AB040907; BAA95998.1; -; mRNA.
DR EMBL; AL136805; CAB66739.1; ALT_INIT; mRNA.
DR EMBL; BC127095; AAI27096.1; ALT_INIT; mRNA.
DR EMBL; BC127096; AAI27097.1; ALT_INIT; mRNA.
DR CCDS; CCDS12421.2; -.
DR RefSeq; NP_065907.2; NM_020856.3.
DR PDB; 2DMI; NMR; -; A=202-303.
DR PDBsum; 2DMI; -.
DR AlphaFoldDB; Q63HK5; -.
DR SMR; Q63HK5; -.
DR BioGRID; 121663; 63.
DR CORUM; Q63HK5; -.
DR IntAct; Q63HK5; 49.
DR MINT; Q63HK5; -.
DR STRING; 9606.ENSP00000240587; -.
DR GlyGen; Q63HK5; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q63HK5; -.
DR PhosphoSitePlus; Q63HK5; -.
DR BioMuta; TSHZ3; -.
DR DMDM; 85541971; -.
DR EPD; Q63HK5; -.
DR jPOST; Q63HK5; -.
DR MassIVE; Q63HK5; -.
DR MaxQB; Q63HK5; -.
DR PaxDb; Q63HK5; -.
DR PeptideAtlas; Q63HK5; -.
DR PRIDE; Q63HK5; -.
DR ProteomicsDB; 65878; -.
DR Antibodypedia; 1780; 110 antibodies from 28 providers.
DR DNASU; 57616; -.
DR Ensembl; ENST00000240587.5; ENSP00000240587.4; ENSG00000121297.8.
DR GeneID; 57616; -.
DR KEGG; hsa:57616; -.
DR MANE-Select; ENST00000240587.5; ENSP00000240587.4; NM_020856.4; NP_065907.2.
DR UCSC; uc002nsy.5; human.
DR CTD; 57616; -.
DR DisGeNET; 57616; -.
DR GeneCards; TSHZ3; -.
DR HGNC; HGNC:30700; TSHZ3.
DR HPA; ENSG00000121297; Tissue enhanced (ovary).
DR MIM; 614119; gene.
DR neXtProt; NX_Q63HK5; -.
DR OpenTargets; ENSG00000121297; -.
DR PharmGKB; PA134887020; -.
DR VEuPathDB; HostDB:ENSG00000121297; -.
DR eggNOG; ENOG502RJS7; Eukaryota.
DR GeneTree; ENSGT00950000183051; -.
DR HOGENOM; CLU_010469_0_0_1; -.
DR InParanoid; Q63HK5; -.
DR OMA; KELVKPM; -.
DR OrthoDB; 106971at2759; -.
DR PhylomeDB; Q63HK5; -.
DR TreeFam; TF328447; -.
DR PathwayCommons; Q63HK5; -.
DR SignaLink; Q63HK5; -.
DR SIGNOR; Q63HK5; -.
DR BioGRID-ORCS; 57616; 9 hits in 1094 CRISPR screens.
DR ChiTaRS; TSHZ3; human.
DR EvolutionaryTrace; Q63HK5; -.
DR GeneWiki; TSHZ3; -.
DR GenomeRNAi; 57616; -.
DR Pharos; Q63HK5; Tbio.
DR PRO; PR:Q63HK5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q63HK5; protein.
DR Bgee; ENSG00000121297; Expressed in cortical plate and 150 other tissues.
DR ExpressionAtlas; Q63HK5; baseline and differential.
DR Genevisible; Q63HK5; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR027008; Teashirt_fam.
DR InterPro; IPR026810; Tshz3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12487; PTHR12487; 1.
DR PANTHER; PTHR12487:SF5; PTHR12487:SF5; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Developmental protein;
KW DNA-binding; Homeobox; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1081
FT /note="Teashirt homolog 3"
FT /id="PRO_0000047066"
FT ZN_FING 214..238
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 275..299
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..404
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 891..961
FT /note="Homeobox; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 976..998
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1041..1064
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 141..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 606..630
FT /evidence="ECO:0000255"
FT COMPBIAS 330..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VARIANT 469
FT /note="E -> G (in dbSNP:rs143453460)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:19745106"
FT /id="VAR_063635"
FT VARIANT 687
FT /note="P -> L (in dbSNP:rs4805664)"
FT /id="VAR_052708"
FT MUTAGEN 953..955
FT /note="VKY->ATA: Does not inhibit interaction with APBB1."
FT /evidence="ECO:0000269|PubMed:19343227"
FT CONFLICT 176
FT /note="L -> V (in Ref. 4; AAI27096/AAI27097)"
FT /evidence="ECO:0000305"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:2DMI"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2DMI"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:2DMI"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2DMI"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:2DMI"
FT TURN 297..301
FT /evidence="ECO:0007829|PDB:2DMI"
SQ SEQUENCE 1081 AA; 118566 MW; B4E0A4347B04E74A CRC64;
MPRRKQQAPR RAAAYVSEEL KAAALVDEGL DPEEHTADGE PSAKYMCPEK ELARACPSYQ
NSPAAEFSCH EMDSESHISE TSDRMADFES GSIKNEEETK EVTVPLEDTT VSDSLEQMKA
VYNNFLSNSY WSNLNLNLHQ PSSEKNNGSS SSSSSSSSSC GSGSFDWHQS AMAKTLQQVS
QSRMLPEPSL FSTVQLYRQS SKLYGSIFTG ASKFRCKDCS AAYDTLVELT VHMNETGHYR
DDNHETDNNN PKRWSKPRKR SLLEMEGKED AQKVLKCMYC GHSFESLQDL SVHMIKTKHY
QKVPLKEPVT PVAAKIIPAT RKKASLELEL PSSPDSTGGT PKATISDTND ALQKNSNPYI
TPNNRYGHQN GASYAWHFEA RKSQILKCME CGSSHDTLQE LTAHMMVTGH FIKVTNSAMK
KGKPIVETPV TPTITTLLDE KVQSVPLAAT TFTSPSNTPA SISPKLNVEV KKEVDKEKAV
TDEKPKQKDK PGEEEEKCDI SSKYHYLTEN DLEESPKGGL DILKSLENTV TSAINKAQNG
TPSWGGYPSI HAAYQLPNMM KLSLGSSGKS TPLKPMFGNS EIVSPTKNQT LVSPPSSQTS
PMPKTNFHAM EELVKKVTEK VAKVEEKMKE PDGKLSPPKR ATPSPCSSEV GEPIKMEASS
DGGFRSQENS PSPPRDGCKD GSPLAEPVEN GKELVKPLAS SLSGSTAIIT DHPPEQPFVN
PLSALQSVMN IHLGKAAKPS LPALDPMSML FKMSNSLAEK AAVATPPPLQ SKKADHLDRY
FYHVNNDQPI DLTKGKSDKG CSLGSVLLSP TSTAPATSSS TVTTAKTSAV VSFMSNSPLR
ENALSDISDM LKNLTESHTS KSSTPSSISE KSDIDGATLE EAEESTPAQK RKGRQSNWNP
QHLLILQAQF AASLRQTSEG KYIMSDLSPQ ERMHISRFTG LSMTTISHWL ANVKYQLRRT
GGTKFLKNLD TGHPVFFCND CASQIRTPST YISHLESHLG FRLRDLSKLS TEQINSQIAQ
TKSPSEKMVT SSPEEDLGTS YQCKLCNRTF ASKHAVKLHL SKTHGKSPED HLLYVSELEK
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