EFCB6_HUMAN
ID EFCB6_HUMAN Reviewed; 1501 AA.
AC Q5THR3; A8K8P6; A8K8Y3; B0QYI4; B0QYI6; Q5U5T6; Q9BY88; Q9H5C4; Q9NSF5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=EF-hand calcium-binding domain-containing protein 6;
DE AltName: Full=CAP-binding protein complex-interacting protein 1;
DE AltName: Full=DJ-1-binding protein;
DE Short=DJBP;
GN Name=EFCAB6 {ECO:0000312|HGNC:HGNC:24204}; Synonyms=DJBP, KIAA1672;
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 [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH PARK7 AND AR, AND VARIANT VAL-1059.
RC TISSUE=Testis;
RX PubMed=12612053;
RA Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
RT "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen
RT receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes
RT this inhibition by abrogation of this complex.";
RL Mol. Cancer Res. 1:247-261(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP ALA-351; TYR-400; ALA-680 AND VAL-1059.
RC TISSUE=Lung, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-1059.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 855-1501 (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1160-1260.
RA Honbou K., Suzuki N.N., Horiuchi M., Taira T., Niki T., Ariga H.,
RA Inagaki F.;
RT "Crystal structure of DJBP fragment which was obtained by limited
RT proteolysis.";
RL Submitted (AUG-2005) to the PDB data bank.
CC -!- FUNCTION: Negatively regulates the androgen receptor by recruiting
CC histone deacetylase complex, and protein DJ-1 antagonizes this
CC inhibition by abrogation of this complex (PubMed:12612053). Microtubule
CC inner protein (MIP) part of the dynein-decorated doublet microtubules
CC (DMTs) in cilia axoneme, which is required for motile cilia beating
CC (Probable). {ECO:0000269|PubMed:12612053, ECO:0000305}.
CC -!- SUBUNIT: Binds PARK7. Part of a ternary complex containing PARK7,
CC EFCAB6/DJBP and AR.
CC -!- INTERACTION:
CC Q5THR3-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12282559, EBI-618309;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12612053}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q5THR3-1; Sequence=Displayed;
CC Name=2; Synonyms=Isoform b;
CC IsoId=Q5THR3-2; Sequence=VSP_019810;
CC Name=3;
CC IsoId=Q5THR3-3; Sequence=VSP_019809;
CC Name=4;
CC IsoId=Q5THR3-4; Sequence=VSP_019808, VSP_019811;
CC Name=6;
CC IsoId=Q5THR3-6; Sequence=VSP_034831, VSP_034832;
CC Name=5;
CC IsoId=Q5THR3-5; Sequence=VSP_019812, VSP_019813;
CC -!- TISSUE SPECIFICITY: Specifically expressed in the testis.
CC {ECO:0000269|PubMed:12612053}.
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DR EMBL; AB073862; BAB71780.1; -; mRNA.
DR EMBL; AK027241; BAB15703.1; -; mRNA.
DR EMBL; AK292411; BAF85100.1; -; mRNA.
DR EMBL; AK292498; BAF85187.1; -; mRNA.
DR EMBL; AL355841; CAB91065.1; -; mRNA.
DR EMBL; AL023801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL118498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z97055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039315; AAH39315.1; -; mRNA.
DR EMBL; AB051459; BAB33342.1; -; mRNA.
DR CCDS; CCDS14049.1; -. [Q5THR3-1]
DR CCDS; CCDS14050.1; -. [Q5THR3-2]
DR RefSeq; NP_073622.2; NM_022785.3. [Q5THR3-1]
DR RefSeq; NP_942153.1; NM_198856.2. [Q5THR3-2]
DR PDB; 1WLZ; X-ray; 1.60 A; A/B/C/D=1160-1260.
DR PDB; 5D67; X-ray; 2.00 A; A/B/C/D=1160-1260.
DR PDBsum; 1WLZ; -.
DR PDBsum; 5D67; -.
DR AlphaFoldDB; Q5THR3; -.
DR SMR; Q5THR3; -.
DR BioGRID; 122306; 5.
DR CORUM; Q5THR3; -.
DR IntAct; Q5THR3; 1.
DR STRING; 9606.ENSP00000262726; -.
DR iPTMnet; Q5THR3; -.
DR PhosphoSitePlus; Q5THR3; -.
DR BioMuta; EFCAB6; -.
DR DMDM; 74756634; -.
DR EPD; Q5THR3; -.
DR MassIVE; Q5THR3; -.
DR PaxDb; Q5THR3; -.
DR PeptideAtlas; Q5THR3; -.
DR PRIDE; Q5THR3; -.
DR ProteomicsDB; 65162; -. [Q5THR3-1]
DR ProteomicsDB; 65163; -. [Q5THR3-2]
DR ProteomicsDB; 65164; -. [Q5THR3-3]
DR ProteomicsDB; 65165; -. [Q5THR3-4]
DR ProteomicsDB; 65166; -. [Q5THR3-5]
DR ProteomicsDB; 65167; -. [Q5THR3-6]
DR Antibodypedia; 320; 28 antibodies from 10 providers.
DR DNASU; 64800; -.
DR Ensembl; ENST00000262726.12; ENSP00000262726.7; ENSG00000186976.15. [Q5THR3-1]
DR Ensembl; ENST00000396231.6; ENSP00000379533.2; ENSG00000186976.15. [Q5THR3-2]
DR GeneID; 64800; -.
DR KEGG; hsa:64800; -.
DR MANE-Select; ENST00000262726.12; ENSP00000262726.7; NM_022785.4; NP_073622.2.
DR UCSC; uc003bdy.3; human. [Q5THR3-1]
DR CTD; 64800; -.
DR DisGeNET; 64800; -.
DR GeneCards; EFCAB6; -.
DR HGNC; HGNC:24204; EFCAB6.
DR HPA; ENSG00000186976; Tissue enhanced (testis).
DR MIM; 619664; gene.
DR neXtProt; NX_Q5THR3; -.
DR OpenTargets; ENSG00000186976; -.
DR PharmGKB; PA162384324; -.
DR VEuPathDB; HostDB:ENSG00000186976; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000013629; -.
DR HOGENOM; CLU_004260_0_0_1; -.
DR InParanoid; Q5THR3; -.
DR OMA; IHWKYFL; -.
DR OrthoDB; 193070at2759; -.
DR PhylomeDB; Q5THR3; -.
DR TreeFam; TF329179; -.
DR PathwayCommons; Q5THR3; -.
DR SignaLink; Q5THR3; -.
DR BioGRID-ORCS; 64800; 4 hits in 1071 CRISPR screens.
DR ChiTaRS; EFCAB6; human.
DR EvolutionaryTrace; Q5THR3; -.
DR GeneWiki; EFCAB6; -.
DR GenomeRNAi; 64800; -.
DR Pharos; Q5THR3; Tdark.
DR PRO; PR:Q5THR3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q5THR3; protein.
DR Bgee; ENSG00000186976; Expressed in left testis and 107 other tissues.
DR ExpressionAtlas; Q5THR3; baseline and differential.
DR Genevisible; Q5THR3; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR015070; EF_hand_DJBP.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF08976; EF-hand_11; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 12.
DR SUPFAM; SSF47473; SSF47473; 7.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 17.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell projection; Cytoplasm;
KW Cytoskeleton; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1501
FT /note="EF-hand calcium-binding domain-containing protein 6"
FT /id="PRO_0000246024"
FT DOMAIN 70..105
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 172..207
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 297..332
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 403..438
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 439..474
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 504..539
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 634..669
FT /note="EF-hand 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 741..776
FT /note="EF-hand 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 847..882
FT /note="EF-hand 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 883..918
FT /note="EF-hand 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 964..999
FT /note="EF-hand 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1069..1104
FT /note="EF-hand 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1176..1211
FT /note="EF-hand 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1212..1247
FT /note="EF-hand 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1359..1394
FT /note="EF-hand 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1434..1469
FT /note="EF-hand 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1470..1501
FT /note="EF-hand 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1501
FT /note="Interaction with PARK7"
FT /evidence="ECO:0000269|PubMed:12612053"
FT REGION 1407..1501
FT /note="Interaction with AR"
FT /evidence="ECO:0000269|PubMed:12612053"
FT COMPBIAS 27..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 754
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 756
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 758
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 765
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 884
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1E8"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1E8"
FT MOD_RES 1294
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1E8"
FT MOD_RES 1304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1E8"
FT VAR_SEQ 1..1139
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12529303"
FT /id="VSP_019808"
FT VAR_SEQ 1..931
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12612053,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_019809"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019810"
FT VAR_SEQ 418..420
FT /note="KPD -> VRF (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_034831"
FT VAR_SEQ 421..1501
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_034832"
FT VAR_SEQ 1140
FT /note="E -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12529303"
FT /id="VSP_019811"
FT VAR_SEQ 1217..1249
FT /note="FDRLWNEMPVNAKGRLKYPDFLSRFSSETAATP -> VRNASQSSPCTPLAE
FT RQPGPWPECTEFKTVLYF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11258795"
FT /id="VSP_019812"
FT VAR_SEQ 1250..1501
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11258795"
FT /id="VSP_019813"
FT VARIANT 166
FT /note="V -> A (in dbSNP:rs16990981)"
FT /id="VAR_048648"
FT VARIANT 199
FT /note="R -> G (in dbSNP:rs3747203)"
FT /id="VAR_048649"
FT VARIANT 351
FT /note="T -> A (in dbSNP:rs5764214)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048650"
FT VARIANT 384
FT /note="S -> A (in dbSNP:rs6006438)"
FT /id="VAR_048651"
FT VARIANT 400
FT /note="H -> Y (in dbSNP:rs137794)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048652"
FT VARIANT 680
FT /note="T -> A (in dbSNP:rs137731)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048653"
FT VARIANT 780
FT /note="D -> N (in dbSNP:rs12159591)"
FT /id="VAR_048654"
FT VARIANT 800
FT /note="R -> W (in dbSNP:rs6006514)"
FT /id="VAR_048655"
FT VARIANT 1059
FT /note="A -> V (in dbSNP:rs9614382)"
FT /evidence="ECO:0000269|PubMed:12612053,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_048656"
FT CONFLICT 478
FT /note="S -> P (in Ref. 2; BAF85187)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="I -> V (in Ref. 2; BAF85187)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="A -> V (in Ref. 2; BAF85187)"
FT /evidence="ECO:0000305"
FT CONFLICT 882
FT /note="P -> S (in Ref. 2; BAF85100)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="Q -> H (in Ref. 1; BAB71780 and 2; BAB15703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1082
FT /note="D -> G (in Ref. 5; AAH39315)"
FT /evidence="ECO:0000305"
FT CONFLICT 1139
FT /note="E -> G (in Ref. 2; BAF85100)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="T -> P (in Ref. 2; BAF85187)"
FT /evidence="ECO:0000305"
FT CONFLICT 1218
FT /note="D -> G (in Ref. 5; AAH39315)"
FT /evidence="ECO:0000305"
FT HELIX 1164..1176
FT /evidence="ECO:0007829|PDB:1WLZ"
FT HELIX 1178..1188
FT /evidence="ECO:0007829|PDB:1WLZ"
FT STRAND 1194..1196
FT /evidence="ECO:0007829|PDB:5D67"
FT HELIX 1198..1208
FT /evidence="ECO:0007829|PDB:1WLZ"
FT HELIX 1214..1221
FT /evidence="ECO:0007829|PDB:1WLZ"
FT HELIX 1234..1241
FT /evidence="ECO:0007829|PDB:1WLZ"
SQ SEQUENCE 1501 AA; 172930 MW; 1D380F63D7FA8FF9 CRC64;
MCKMAIIPDW LRSHPHTRKF THSRPHSSPC RVYSRNGSPN KFRSSSTTAV ANPTLSSLDV
KRILFQKITD RGDELQKAFQ LLDTGQNLTV SKSELRRIIT DFLMPLTREQ FQDVLAQIPL
STSGTVPYLA FLSRFGGIDL YINGIKRGGG NEMNCCRTLR ELEIQVGEKV FKNIKTVMKA
FELIDVNKTG LVRPQELRRV LETFCMKLRD EEYEKFSKHY NIHKDTAVDY NVFLKNLSIN
NDLNLRYCMG NQEVSLENQQ AKNSKKERLL GSASSEDIWR NYSLDEIERN FCLQLSKSYE
KVEKALSAGD PCKGGYVSFN YLKIVLDTFV YQIPRRIFIQ LMKRFGLKAT TKINWKQFLT
SFHEPQGLQV SSKGPLTKRN SINSRNESHK ENIITKLFRH TEDHSASLKK ALLIINTKPD
GPITREEFRY ILNCMAVKLS DSEFKELMQM LDPGDTGVVN TSMFIDLIEE NCRMRKTSPC
TDAKTPFLLA WDSVEEIVHD TITRNLQAFY NMLRSYDLGD TGRIGRNNFK KIMHVFCPFL
TNAHFIKLCS KIQDIGSGRI LYKKLLACIG IDGPPTVSPV LVPKDQLLSE HLQKDEQQQP
DLSERTKLTE DKTTLTKKMT TEEVIEKFKK CIQQQDPAFK KRFLDFSKEP NGKINVHDFK
KVLEDTGMPM DDDQYALLTT KIGFEKEGMS YLDFAAGFED PPMRGPETTP PQPPTPSKSY
VNSHFITAEE CLKLFPRRLK ESFRDPYSAF FKTDADRDGI INMHDLHRLL LHLLLNLKDD
EFERFLGLLG LRLSVTLNFR EFQNLCEKRP WRTDEAPQRL IRPKQKVADS ELACEQAHQY
LVTKAKNRWS DLSKNFLETD NEGNGILRRR DIKNALYGFD IPLTPREFEK LWARYDTEGK
GHITYQEFLQ KLGINYSPAV HRPCAEDYFN FMGHFTKPQQ LQEEMKELQQ STEKAVAARD
KLMDRHQDIS KAFTKTDQSK TNYISICKMQ EVLEECGCSL TEGELTHLLN SWGVSRHDNA
INYLDFLRAV ENSKSTGAQP KEKEESMPIN FATLNPQEAV RKIQEVVESS QLALSTAFSA
LDKEDTGFVK ATEFGQVLKD FCYKLTDNQY HYFLRKLRIH LTPYINWKYF LQNFSCFLEE
TADEWAEKMP KGPPPTSPKA TADRDILARL HKAVTSHYHA ITQEFENFDT MKTNTISREE
FRAICNRRVQ ILTDEQFDRL WNEMPVNAKG RLKYPDFLSR FSSETAATPM ATGDSAVAQR
GSSVPDVSEG TRSALSLPTQ ELRPGSKSQS HPCTPASTTV IPGTPPLQNC DPIESRLRKR
IQGCWRQLLK ECKEKDVARQ GDINASDFLA LVEKFNLDIS KEECQQLIIK YDLKSNGKFA
YCDFIQSCVL LLKAKESSLM HRMKIQNAHK MKEAGAETPS FYSALLRIQP KIVHCWRPMR
RTFKSYDEAG TGLLSVADFR TVLRQYSINL SEEEFFHILE YYDKTLSSKI SYNDFLRAFL
Q
