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 27-MAR-2024, entry version 168. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 48. DR IntAct; Q8NHU6; 27. DR MINT; Q8NHU6; -. DR STRING; 9606.ENSP00000347444; -. DR ChEMBL; CHEMBL4105828; -. DR GlyGen; Q8NHU6; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000347444; -. DR PeptideAtlas; Q8NHU6; -. DR ProteomicsDB; 73759; -. [Q8NHU6-1] DR ProteomicsDB; 73760; -. [Q8NHU6-2] DR ProteomicsDB; 73761; -. [Q8NHU6-3] DR Pumba; Q8NHU6; -. DR Antibodypedia; 14331; 102 antibodies from 22 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 AGR; HGNC:30831; -. 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; CKGKWSR; -. DR OrthoDB; 5403690at2759; -. DR PhylomeDB; Q8NHU6; -. DR PathwayCommons; Q8NHU6; -. DR SignaLink; Q8NHU6; -. DR BioGRID-ORCS; 23424; 7 hits in 1158 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 203 other cell types or tissues. DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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: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 processing; 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; cd09986; LOTUS_1_TDRD7; 1. DR CDD; cd09973; LOTUS_2_TDRD7; 1. DR CDD; cd09974; LOTUS_3_TDRD7; 1. DR CDD; cd20427; Tudor_TDRD7_rpt1; 1. DR CDD; cd20428; Tudor_TDRD7_rpt2; 1. DR CDD; cd20429; Tudor_TDRD7_rpt3; 1. DR Gene3D; 2.30.30.140; -; 3. DR Gene3D; 2.40.50.90; -; 3. DR Gene3D; 3.30.420.610; LOTUS domain-like; 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 InterPro; IPR047448; Tudor_TDRD7_rpt2. DR InterPro; IPR047449; Tudor_TDRD7_rpt3. DR PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1. DR PANTHER; PTHR22948:SF29; TUDOR DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF12872; OST-HTH; 2. DR Pfam; PF00567; TUDOR; 3. DR SMART; SM00333; TUDOR; 2. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 3. DR PROSITE; PS51644; HTH_OST; 3. DR PROSITE; PS50304; TUDOR; 2. DR Genevisible; Q8NHU6; HS. 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 //