TDRD7_HUMAN
ID TDRD7_HUMAN Reviewed; 1098 AA.
AC Q8NHU6; A6NCI6; B2RBX3; B4DG99; B4DXF7; E7EQD4; Q5VV27; Q96JT1; Q9UFF0;
AC Q9Y2M3;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Tudor domain-containing protein 7;
DE AltName: Full=PCTAIRE2-binding protein;
DE AltName: Full=Tudor repeat associator with PCTAIRE-2;
DE Short=Trap;
GN Name=TDRD7; Synonyms=PCTAIRE2BP;
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] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP ALA-150.
RC TISSUE=Amygdala, and 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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-150.
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] (ISOFORM 1), AND VARIANT LEU-456.
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 631-1098.
RC TISSUE=Brain;
RX PubMed=10727952; DOI=10.1046/j.1432-1327.2000.01218.x;
RA Hirose T., Kawabuchi M., Tamaru T., Okumura N., Nagai K., Okada M.;
RT "Identification of tudor repeat associator with PCTAIRE 2 (Trap). A novel
RT protein that interacts with the N-terminal domain of PCTAIRE 2 in rat
RT brain.";
RL Eur. J. Biochem. 267:2113-2121(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 837-1098.
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 [7]
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 [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 IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
RX PubMed=20305267; DOI=10.1093/bioinformatics/btq122;
RA Callebaut I., Mornon J.P.;
RT "LOTUS, a new domain associated with small RNA pathways in the germline.";
RL Bioinformatics 26:1140-1144(2010).
RN [10]
RP IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
RX PubMed=20302647; DOI=10.1186/1745-6150-5-13;
RA Anantharaman V., Zhang D., Aravind L.;
RT "OST-HTH: a novel predicted RNA-binding domain.";
RL Biol. Direct 5:13-13(2010).
RN [11]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND VARIANT CTRCT36 VAL-618
RP DEL.
RX PubMed=21436445; DOI=10.1126/science.1195970;
RA Lachke S.A., Alkuraya F.S., Kneeland S.C., Ohn T., Aboukhalil A.,
RA Howell G.R., Saadi I., Cavallesco R., Yue Y., Tsai A.C., Nair K.S.,
RA Cosma M.I., Smith R.S., Hodges E., Alfadhli S.M., Al-Hajeri A.,
RA Shamseldin H.E., Behbehani A., Hannon G.J., Bulyk M.L., Drack A.V.,
RA Anderson P.J., John S.W., Maas R.L.;
RT "Mutations in the RNA granule component TDRD7 cause cataract and
RT glaucoma.";
RL Science 331:1571-1576(2011).
RN [12]
RP IDENTIFICATION BY MASS 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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).
CC -!- FUNCTION: Component of specific cytoplasmic RNA granules involved in
CC post-transcriptional regulation of specific genes: probably acts by
CC binding to specific mRNAs and regulating their translation. Required
CC for lens transparency during lens development, by regulating
CC translation of genes such as CRYBB3 and HSPB1 in the developing lens.
CC Also required during spermatogenesis. {ECO:0000269|PubMed:21436445}.
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC TDRD7 and DDX4. Found in a complex containing CABLES1, CDK16 and CDK17.
CC Interacts with CABLES1, CDK17 and PIWIL1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8NHU6; P42771: CDKN2A; NbExp=2; IntAct=EBI-624505, EBI-375053;
CC Q8NHU6; Q06547: GABPB1; NbExp=4; IntAct=EBI-624505, EBI-618165;
CC Q8NHU6; O75410: TACC1; NbExp=4; IntAct=EBI-624505, EBI-624237;
CC Q8NHU6; O75410-1: TACC1; NbExp=3; IntAct=EBI-624505, EBI-624252;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21436445}.
CC Note=Localizes to cytoplasmic RNA granules. Present in chromatoid body
CC (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or
CC polar granules in Drosophila germ cells), also named processing bodies
CC (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic
CC CBs (also called intermitochondrial cementin) in pachytene
CC spermatocytes and as a single perinuclear CB in haploid round
CC spermatids (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NHU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NHU6-2; Sequence=VSP_041315;
CC Name=3;
CC IsoId=Q8NHU6-3; Sequence=VSP_041314, VSP_041316;
CC -!- DISEASE: Cataract 36 (CTRCT36) [MIM:613887]: An opacification of the
CC crystalline lens of the eye becoming evident at birth. It frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function.
CC {ECO:0000269|PubMed:21436445}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TDRD7 family. {ECO:0000305}.
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DR EMBL; AK294488; BAG57710.1; -; mRNA.
DR EMBL; AK301954; BAG63369.1; -; mRNA.
DR EMBL; AK314853; BAG37370.1; -; mRNA.
DR EMBL; AL449464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58844.1; -; Genomic_DNA.
DR EMBL; BC028694; AAH28694.1; -; mRNA.
DR EMBL; AB025254; BAA76379.1; -; mRNA.
DR EMBL; AL122110; CAB59271.1; -; mRNA.
DR CCDS; CCDS6725.1; -. [Q8NHU6-1]
DR PIR; T34547; T34547.
DR RefSeq; NP_001289813.1; NM_001302884.1. [Q8NHU6-2]
DR RefSeq; NP_055105.2; NM_014290.2. [Q8NHU6-1]
DR PDB; 3RCO; X-ray; 1.80 A; A/B=1-82.
DR PDBsum; 3RCO; -.
DR AlphaFoldDB; Q8NHU6; -.
DR SMR; Q8NHU6; -.
DR BioGRID; 116994; 45.
DR IntAct; Q8NHU6; 27.
DR MINT; Q8NHU6; -.
DR STRING; 9606.ENSP00000347444; -.
DR ChEMBL; CHEMBL4105828; -.
DR iPTMnet; Q8NHU6; -.
DR PhosphoSitePlus; Q8NHU6; -.
DR BioMuta; TDRD7; -.
DR DMDM; 152031705; -.
DR EPD; Q8NHU6; -.
DR jPOST; Q8NHU6; -.
DR MassIVE; Q8NHU6; -.
DR MaxQB; Q8NHU6; -.
DR PaxDb; Q8NHU6; -.
DR PeptideAtlas; Q8NHU6; -.
DR PRIDE; Q8NHU6; -.
DR ProteomicsDB; 73759; -. [Q8NHU6-1]
DR ProteomicsDB; 73760; -. [Q8NHU6-2]
DR ProteomicsDB; 73761; -. [Q8NHU6-3]
DR Antibodypedia; 14331; 89 antibodies from 20 providers.
DR DNASU; 23424; -.
DR Ensembl; ENST00000355295.5; ENSP00000347444.4; ENSG00000196116.8. [Q8NHU6-1]
DR GeneID; 23424; -.
DR KEGG; hsa:23424; -.
DR MANE-Select; ENST00000355295.5; ENSP00000347444.4; NM_014290.3; NP_055105.2.
DR UCSC; uc004axj.4; human. [Q8NHU6-1]
DR CTD; 23424; -.
DR DisGeNET; 23424; -.
DR GeneCards; TDRD7; -.
DR HGNC; HGNC:30831; TDRD7.
DR HPA; ENSG00000196116; Tissue enhanced (retina).
DR MalaCards; TDRD7; -.
DR MIM; 611258; gene.
DR MIM; 613887; phenotype.
DR neXtProt; NX_Q8NHU6; -.
DR OpenTargets; ENSG00000196116; -.
DR PharmGKB; PA134937960; -.
DR VEuPathDB; HostDB:ENSG00000196116; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00890000139482; -.
DR HOGENOM; CLU_283554_0_0_1; -.
DR InParanoid; Q8NHU6; -.
DR OMA; VMAGDFK; -.
DR OrthoDB; 1276848at2759; -.
DR PhylomeDB; Q8NHU6; -.
DR PathwayCommons; Q8NHU6; -.
DR SignaLink; Q8NHU6; -.
DR BioGRID-ORCS; 23424; 7 hits in 1079 CRISPR screens.
DR ChiTaRS; TDRD7; human.
DR GeneWiki; TDRD7; -.
DR GenomeRNAi; 23424; -.
DR Pharos; Q8NHU6; Tbio.
DR PRO; PR:Q8NHU6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8NHU6; protein.
DR Bgee; ENSG00000196116; Expressed in secondary oocyte and 201 other tissues.
DR Genevisible; Q8NHU6; HS.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0070306; P:lens fiber cell differentiation; IMP:UniProtKB.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:UniProtKB.
DR GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd09974; LOTUS_3_TDRD7; 1.
DR CDD; cd04508; TUDOR; 3.
DR Gene3D; 2.40.50.90; -; 3.
DR Gene3D; 3.30.420.610; -; 3.
DR InterPro; IPR041966; LOTUS-like.
DR InterPro; IPR025605; OST-HTH/LOTUS_dom.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR037978; TDRD7_LOTUS_3.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF12872; OST-HTH; 2.
DR Pfam; PF00567; TUDOR; 3.
DR SMART; SM00333; TUDOR; 2.
DR PROSITE; PS51644; HTH_OST; 3.
DR PROSITE; PS50304; TUDOR; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cataract; Cytoplasm; Differentiation;
KW Disease variant; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Spermatogenesis.
FT CHAIN 1..1098
FT /note="Tudor domain-containing protein 7"
FT /id="PRO_0000183169"
FT DOMAIN 3..76
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 233..302
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 337..406
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 513..570
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 703..760
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 129..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..1098
FT /note="Interaction with CDK17"
FT /evidence="ECO:0000250"
FT REGION 893..1098
FT /note="Interaction with CABLES1"
FT /evidence="ECO:0000250"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1H1"
FT VAR_SEQ 1..651
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041314"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041315"
FT VAR_SEQ 694..722
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041316"
FT VARIANT 150
FT /note="V -> A (in dbSNP:rs2045732)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT /id="VAR_019070"
FT VARIANT 456
FT /note="P -> L (in dbSNP:rs17852595)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033044"
FT VARIANT 618
FT /note="Missing (in CTRCT36; dbSNP:rs750207077)"
FT /evidence="ECO:0000269|PubMed:21436445"
FT /id="VAR_065247"
FT CONFLICT 659
FT /note="T -> A (in Ref. 1; BAG63369)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:3RCO"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:3RCO"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:3RCO"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:3RCO"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3RCO"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3RCO"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3RCO"
SQ SEQUENCE 1098 AA; 123586 MW; F27E383E5B18C428 CRC64;
MLEGDLVSKM LRAVLQSHKN GVALPRLQGE YRSLTGDWIP FKQLGFPTLE AYLRSVPAVV
RIETSRSGEI TCYAMACTET ARIAQLVARQ RSSKRKTGRQ VNCQMRVKKT MPFFLEGKPK
ATLRQPGFAS NFSVGKKPNP APLRDKGNSV GVKPDAEMSP YMLHTTLGNE AFKDIPVQRH
VTMSTNNRFS PKASLQPPLQ MHLSRTSTKE MSDNLNQTVE KPNVKPPASY TYKMDEVQNR
IKEILNKHNN GIWISKLPHF YKELYKEDLN QGILQQFEHW PHICTVEKPC SGGQDLLLYP
AKRKQLLRSE LDTEKVPLSP LPGPKQTPPL KGCPTVMAGD FKEKVADLLV KYTSGLWASA
LPKAFEEMYK VKFPEDALKN LASLSDVCSI DYISGNPQKA ILYAKLPLPT DKIQKDAGQA
HGDNDIKAMV EQEYLQVEES IAESANTFME DITVPPLMIP TEASPSVLVV ELSNTNEVVI
RYVGKDYSAA QELMEDEMKE YYSKNPKITP VQAVNVGQLL AVNAEEDAWL RAQVISTEEN
KIKVCYVDYG FSENVEKSKA YKLNPKFCSL SFQATKCKLA GLEVLSDDPD LVKVVESLTC
GKIFAVEILD KADIPLVVLY DTSGEDDINI NATCLKAICD KSLEVHLQVD AMYTNVKVTN
ICSDGTLYCQ VPCKGLNKLS DLLRKIEDYF HCKHMTSECF VSLPFCGKIC LFHCKGKWLR
VEITNVHSSR ALDVQFLDSG TVTSVKVSEL REIPPRFLQE MIAIPPQAIK CCLADLPQSI
GMWTPDAVLW LRDSVLNCSD CSIKVTKVDE TRGIAHVYLF TPKNFPDPHR SINRQITNAD
LWKHQKDVFL SAISSGADSP NSKNGNMPMS GNTGENFRKN LTDVIKKSMV DHTSAFSTEE
LPPPVHLSKP GEHMDVYVPV ACHPGYFVIQ PWQEIHKLEV LMEEMILYYS VSEERHIAVE
KDQVYAAKVE NKWHRVLLKG ILTNGLVSVY ELDYGKHELV NIRKVQPLVD MFRKLPFQAV
TAQLAGVKCN QWSEEASMVF RNHVEKKPLV ALVQTVIENA NPWDRKVVVY LVDTSLPDTD
TWIHDFMSEY LIELSKVN
