CTC1_HUMAN
ID CTC1_HUMAN Reviewed; 1217 AA.
AC Q2NKJ3; B3KR66; C9JEX5; Q1PCD1; Q2TBE3; Q8N3S6; Q9H6L0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=CST complex subunit CTC1;
DE AltName: Full=Conserved telomere maintenance component 1;
DE AltName: Full=HBV DNAPTP1-transactivated protein B;
GN Name=CTC1; Synonyms=C17orf68;
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 1), AND VARIANT VAL-1005.
RA Lun Y.Z., Cheng J., Guo J., Zhang L.Y., Zhao B.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-1005.
RC TISSUE=Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-1005.
RC TISSUE=Corpus callosum, and Kidney epithelium;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-1005.
RC TISSUE=Lung carcinoma, and Uterine adenocarcinoma;
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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CST
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=19854130; DOI=10.1016/j.molcel.2009.08.009;
RA Miyake Y., Nakamura M., Nabetani A., Shimamura S., Tamura M., Yonehara S.,
RA Saito M., Ishikawa F.;
RT "RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and
RT protects telomeres independently of the Pot1 pathway.";
RL Mol. Cell 36:193-206(2009).
RN [7]
RP FUNCTION.
RX PubMed=19854131; DOI=10.1016/j.molcel.2009.09.017;
RA Surovtseva Y.V., Churikov D., Boltz K.A., Song X., Lamb J.C.,
RA Warrington R., Leehy K., Heacock M., Price C.M., Shippen D.E.;
RT "Conserved telomere maintenance component 1 interacts with STN1 and
RT maintains chromosome ends in higher eukaryotes.";
RL Mol. Cell 36:207-218(2009).
RN [8]
RP FUNCTION, AND FUNCTION OF THE CST COMPLEX.
RX PubMed=22863775; DOI=10.1038/emboj.2012.215;
RA Stewart J.A., Wang F., Chaiken M.F., Kasbek C., Chastain P.D. II,
RA Wright W.E., Price C.M.;
RT "Human CST promotes telomere duplex replication and general replication
RT restart after fork stalling.";
RL EMBO J. 31:3537-3549(2012).
RN [9]
RP FUNCTION OF THE CST COMPLEX, AND INTERACTION WITH STN1; ACD AND POT1.
RX PubMed=22763445; DOI=10.1038/nature11269;
RA Chen L.Y., Redon S., Lingner J.;
RT "The human CST complex is a terminator of telomerase activity.";
RL Nature 488:540-544(2012).
RN [10]
RP FUNCTION OF THE CST COMPLEX.
RX PubMed=25483097; DOI=10.4161/15384101.2014.964100;
RA Wang F., Stewart J., Price C.M.;
RT "Human CST abundance determines recovery from diverse forms of DNA damage
RT and replication stress.";
RL Cell Cycle 13:3488-3498(2014).
RN [11]
RP VARIANTS CRMCC1 VAL-227; GLY-665; GLY-975; CYS-985 DEL; HIS-1142 AND
RP 1196-LEU--ARG-1202 DEL.
RX PubMed=22387016; DOI=10.1016/j.ajhg.2012.02.002;
RA Polvi A., Linnankivi T., Kivela T., Herva R., Keating J.P., Makitie O.,
RA Pareyson D., Vainionpaa L., Lahtinen J., Hovatta I., Pihko H.,
RA Lehesjoki A.E.;
RT "Mutations in CTC1, encoding the CTS telomere maintenance complex component
RT 1, cause cerebroretinal microangiopathy with calcifications and cysts.";
RL Am. J. Hum. Genet. 90:540-549(2012).
RN [12]
RP VARIANTS CRMCC1 MET-259; ARG-503; TRP-840; MET-871; GLY-975; CYS-985 DEL;
RP TRP-987 AND 1196-LEU--ARG-1202 DEL.
RX PubMed=22267198; DOI=10.1038/ng.1084;
RA Anderson B.H., Kasher P.R., Mayer J., Szynkiewicz M., Jenkinson E.M.,
RA Bhaskar S.S., Urquhart J.E., Daly S.B., Dickerson J.E., O'Sullivan J.,
RA Leibundgut E.O., Muter J., Abdel-Salem G.M., Babul-Hirji R., Baxter P.,
RA Berger A., Bonafe L., Brunstom-Hernandez J.E., Buckard J.A., Chitayat D.,
RA Chong W.K., Cordelli D.M., Ferreira P., Fluss J., Forrest E.H.,
RA Franzoni E., Garone C., Hammans S.R., Houge G., Hughes I., Jacquemont S.,
RA Jeannet P.Y., Jefferson R.J., Kumar R., Kutschke G., Lundberg S.,
RA Lourenco C.M., Mehta R., Naidu S., Nischal K.K., Nunes L., Ounap K.,
RA Philippart M., Prabhakar P., Risen S.R., Schiffmann R., Soh C.,
RA Stephenson J.B., Stewart H., Stone J., Tolmie J.L., van der Knaap M.S.,
RA Vieira J.P., Vilain C.N., Wakeling E.L., Wermenbol V., Whitney A.,
RA Lovell S.C., Meyer S., Livingston J.H., Baerlocher G.M., Black G.C.,
RA Rice G.I., Crow Y.J.;
RT "Mutations in CTC1, encoding conserved telomere maintenance component 1,
RT cause Coats plus.";
RL Nat. Genet. 44:338-342(2012).
CC -!- FUNCTION: Component of the CST complex proposed to act as a specialized
CC replication factor promoting DNA replication under conditions of
CC replication stress or natural replication barriers such as the telomere
CC duplex. The CST complex binds single-stranded DNA with high affinity in
CC a sequence-independent manner, while isolated subunits bind DNA with
CC low affinity by themselves. Initially the CST complex has been proposed
CC to protect telomeres from DNA degradation (PubMed:19854130). However,
CC the CST complex has been shown to be involved in several aspects of
CC telomere replication. The CST complex inhibits telomerase and is
CC involved in telomere length homeostasis; it is proposed to bind to
CC newly telomerase-synthesized 3' overhangs and to terminate telomerase
CC action implicating the association with the ACD:POT1 complex thus
CC interfering with its telomerase stimulation activity. The CST complex
CC is also proposed to be involved in fill-in synthesis of the telomeric
CC C-strand probably implicating recruitment and activation of DNA
CC polymerase alpha (PubMed:22763445). The CST complex facilitates
CC recovery from many forms of exogenous DNA damage; seems to be involved
CC in the re-initiation of DNA replication at repaired forks and/or
CC dormant origins (PubMed:25483097). Involved in telomere maintenance
CC (PubMed:19854131, PubMed:22863775). Involved in genome stability
CC (PubMed:22863775). May be in involved in telomeric C-strand fill-in
CC during late S/G2 phase (By similarity). {ECO:0000250|UniProtKB:Q5SUQ9,
CC ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:19854131,
CC ECO:0000269|PubMed:22763445, ECO:0000269|PubMed:22863775,
CC ECO:0000269|PubMed:25483097}.
CC -!- SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106,
CC CTC1/C17orf68 and STN1; in the complex interacts directly with STN1.
CC Interacts with ACD and POT1. {ECO:0000269|PubMed:19854130,
CC ECO:0000269|PubMed:22763445}.
CC -!- INTERACTION:
CC Q2NKJ3; Q92624: APPBP2; NbExp=3; IntAct=EBI-2562802, EBI-743771;
CC Q2NKJ3; Q9H668: STN1; NbExp=7; IntAct=EBI-2562802, EBI-746930;
CC Q2NKJ3; Q86WV5: TEN1; NbExp=3; IntAct=EBI-2562802, EBI-2562799;
CC Q2NKJ3-1; Q9H668: STN1; NbExp=5; IntAct=EBI-15994382, EBI-746930;
CC Q2NKJ3-1; O14773-1: TPP1; NbExp=3; IntAct=EBI-15994382, EBI-15619703;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19854130}.
CC Chromosome, telomere {ECO:0000269|PubMed:19854130}. Note=A
CC transmembrane region is predicted by sequence analysis tools (ESKW,
CC MEMSAT and Phobius); however, given the telomeric localization of the
CC protein, the relevance of the transmembrane region is unsure in vivo.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2NKJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2NKJ3-2; Sequence=VSP_025351, VSP_025352, VSP_025353;
CC -!- DISEASE: Cerebroretinal microangiopathy with calcifications and cysts 1
CC (CRMCC1) [MIM:612199]: An autosomal recessive pleiomorphic disorder
CC characterized primarily by intracranial calcifications, leukodystrophy,
CC and brain cysts, resulting in spasticity, ataxia, dystonia, seizures,
CC and cognitive decline. Patients also have retinal telangiectasia and
CC exudates (Coats disease) as well as extraneurologic manifestations,
CC including osteopenia with poor bone healing and a high risk of
CC gastrointestinal bleeding and portal hypertension caused by vasculature
CC ectasias in the stomach, small intestine, and liver. Some individuals
CC also have hair, skin, and nail changes, as well as anemia and
CC thrombocytopenia. {ECO:0000269|PubMed:22267198,
CC ECO:0000269|PubMed:22387016}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CTC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38600.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ451688; ABE02809.1; -; mRNA.
DR EMBL; AL831955; CAD38600.1; ALT_INIT; mRNA.
DR EMBL; AK091077; BAG52278.1; -; mRNA.
DR EMBL; AC135178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026057; AAH26057.2; -; mRNA.
DR EMBL; BC110373; AAI10374.1; -; mRNA.
DR EMBL; BC111783; AAI11784.1; -; mRNA.
DR EMBL; AK025823; BAB15247.1; ALT_INIT; mRNA.
DR CCDS; CCDS42259.1; -. [Q2NKJ3-1]
DR RefSeq; NP_079375.3; NM_025099.5. [Q2NKJ3-1]
DR PDB; 5W2L; X-ray; 1.86 A; A/B=716-880.
DR PDB; 6W6W; EM; 3.00 A; A/B=2-1217.
DR PDBsum; 5W2L; -.
DR PDBsum; 6W6W; -.
DR AlphaFoldDB; Q2NKJ3; -.
DR SMR; Q2NKJ3; -.
DR BioGRID; 123155; 85.
DR ComplexPortal; CPX-2129; CST complex.
DR CORUM; Q2NKJ3; -.
DR DIP; DIP-56900N; -.
DR IntAct; Q2NKJ3; 20.
DR STRING; 9606.ENSP00000313759; -.
DR iPTMnet; Q2NKJ3; -.
DR PhosphoSitePlus; Q2NKJ3; -.
DR BioMuta; CTC1; -.
DR DMDM; 292495002; -.
DR EPD; Q2NKJ3; -.
DR jPOST; Q2NKJ3; -.
DR MassIVE; Q2NKJ3; -.
DR MaxQB; Q2NKJ3; -.
DR PaxDb; Q2NKJ3; -.
DR PeptideAtlas; Q2NKJ3; -.
DR PRIDE; Q2NKJ3; -.
DR ProteomicsDB; 61406; -. [Q2NKJ3-1]
DR ProteomicsDB; 61407; -. [Q2NKJ3-2]
DR Antibodypedia; 47974; 58 antibodies from 11 providers.
DR DNASU; 80169; -.
DR Ensembl; ENST00000449476.7; ENSP00000396018.2; ENSG00000178971.16. [Q2NKJ3-2]
DR Ensembl; ENST00000651323.1; ENSP00000498499.1; ENSG00000178971.16. [Q2NKJ3-1]
DR GeneID; 80169; -.
DR KEGG; hsa:80169; -.
DR MANE-Select; ENST00000651323.1; ENSP00000498499.1; NM_025099.6; NP_079375.3.
DR UCSC; uc002gkq.5; human. [Q2NKJ3-1]
DR CTD; 80169; -.
DR DisGeNET; 80169; -.
DR GeneCards; CTC1; -.
DR GeneReviews; CTC1; -.
DR HGNC; HGNC:26169; CTC1.
DR HPA; ENSG00000178971; Low tissue specificity.
DR MalaCards; CTC1; -.
DR MIM; 612199; phenotype.
DR MIM; 613129; gene.
DR neXtProt; NX_Q2NKJ3; -.
DR OpenTargets; ENSG00000178971; -.
DR Orphanet; 313838; Coats plus syndrome.
DR Orphanet; 1775; Dyskeratosis congenita.
DR PharmGKB; PA142672251; -.
DR VEuPathDB; HostDB:ENSG00000178971; -.
DR eggNOG; ENOG502RBD3; Eukaryota.
DR GeneTree; ENSGT00390000011553; -.
DR HOGENOM; CLU_008170_0_0_1; -.
DR InParanoid; Q2NKJ3; -.
DR OMA; SMAGFIQ; -.
DR OrthoDB; 1282784at2759; -.
DR PhylomeDB; Q2NKJ3; -.
DR TreeFam; TF335866; -.
DR PathwayCommons; Q2NKJ3; -.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-174430; Telomere C-strand synthesis initiation.
DR SignaLink; Q2NKJ3; -.
DR BioGRID-ORCS; 80169; 243 hits in 1087 CRISPR screens.
DR ChiTaRS; CTC1; human.
DR GenomeRNAi; 80169; -.
DR Pharos; Q2NKJ3; Tbio.
DR PRO; PR:Q2NKJ3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q2NKJ3; protein.
DR Bgee; ENSG00000178971; Expressed in granulocyte and 122 other tissues.
DR ExpressionAtlas; Q2NKJ3; baseline and differential.
DR Genevisible; Q2NKJ3; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:1990879; C:CST complex; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0048539; P:bone marrow development; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0016233; P:telomere capping; TAS:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IBA:GO_Central.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR InterPro; IPR029156; CTC1.
DR InterPro; IPR042617; CTC1-like.
DR PANTHER; PTHR14865; PTHR14865; 1.
DR Pfam; PF15489; CTC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Disease variant;
KW DNA-binding; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..1217
FT /note="CST complex subunit CTC1"
FT /id="PRO_0000287181"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 217..251
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025351"
FT VAR_SEQ 1053..1066
FT /note="GKCTRLGSTCPTQT -> APGGGWDCRSRGDL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025352"
FT VAR_SEQ 1067..1217
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025353"
FT VARIANT 227
FT /note="A -> V (in CRMCC1; dbSNP:rs199473673)"
FT /evidence="ECO:0000269|PubMed:22387016"
FT /id="VAR_067369"
FT VARIANT 259
FT /note="V -> M (in CRMCC1; dbSNP:rs387907080)"
FT /evidence="ECO:0000269|PubMed:22267198"
FT /id="VAR_067370"
FT VARIANT 503
FT /note="G -> R (in CRMCC1; dbSNP:rs1320809462)"
FT /evidence="ECO:0000269|PubMed:22267198"
FT /id="VAR_067371"
FT VARIANT 665
FT /note="V -> G (in CRMCC1; dbSNP:rs199473676)"
FT /evidence="ECO:0000269|PubMed:22387016"
FT /id="VAR_067372"
FT VARIANT 820
FT /note="I -> V (in dbSNP:rs3027238)"
FT /id="VAR_032282"
FT VARIANT 840
FT /note="R -> W (in CRMCC1; dbSNP:rs373905859)"
FT /evidence="ECO:0000269|PubMed:22267198"
FT /id="VAR_067373"
FT VARIANT 871
FT /note="V -> M (in CRMCC1; dbSNP:rs369255297)"
FT /evidence="ECO:0000269|PubMed:22267198"
FT /id="VAR_067374"
FT VARIANT 975
FT /note="R -> G (in CRMCC1; dbSNP:rs199473678)"
FT /evidence="ECO:0000269|PubMed:22267198,
FT ECO:0000269|PubMed:22387016"
FT /id="VAR_067375"
FT VARIANT 985
FT /note="Missing (in CRMCC1)"
FT /evidence="ECO:0000269|PubMed:22267198,
FT ECO:0000269|PubMed:22387016"
FT /id="VAR_067376"
FT VARIANT 987
FT /note="R -> W (in CRMCC1; dbSNP:rs202138550)"
FT /evidence="ECO:0000269|PubMed:22267198"
FT /id="VAR_067377"
FT VARIANT 1005
FT /note="I -> V (in dbSNP:rs3826543)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.1"
FT /id="VAR_032283"
FT VARIANT 1142
FT /note="L -> H (in CRMCC1; dbSNP:rs199473681)"
FT /evidence="ECO:0000269|PubMed:22387016"
FT /id="VAR_067378"
FT VARIANT 1196..1202
FT /note="Missing (in CRMCC1)"
FT /evidence="ECO:0000269|PubMed:22267198,
FT ECO:0000269|PubMed:22387016"
FT /id="VAR_067379"
FT CONFLICT 41
FT /note="L -> V (in Ref. 2; CAD38600)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="L -> P (in Ref. 2; CAD38600)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="S -> I (in Ref. 1; ABE02809 and 3; BAG52278)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="S -> G (in Ref. 2; CAD38600)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="A -> T (in Ref. 5; AAI10374)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="G -> E (in Ref. 2; CAD38600)"
FT /evidence="ECO:0000305"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 464..473
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 474..480
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 621..624
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 629..637
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 650..656
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 658..667
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 681..694
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 728..738
FT /evidence="ECO:0007829|PDB:5W2L"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:5W2L"
FT STRAND 760..769
FT /evidence="ECO:0007829|PDB:5W2L"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:5W2L"
FT STRAND 795..801
FT /evidence="ECO:0007829|PDB:5W2L"
FT HELIX 802..810
FT /evidence="ECO:0007829|PDB:5W2L"
FT STRAND 816..824
FT /evidence="ECO:0007829|PDB:5W2L"
FT TURN 827..831
FT /evidence="ECO:0007829|PDB:5W2L"
FT HELIX 843..845
FT /evidence="ECO:0007829|PDB:5W2L"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:5W2L"
FT STRAND 859..862
FT /evidence="ECO:0007829|PDB:5W2L"
FT HELIX 865..873
FT /evidence="ECO:0007829|PDB:5W2L"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 896..907
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 929..935
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 938..940
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 945..950
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 952..954
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 966..976
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 980..985
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 992..994
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 1012..1015
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1017..1019
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1023..1025
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1028..1038
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1044..1047
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1072..1078
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1085..1088
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 1090..1092
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 1094..1096
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 1101..1107
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1108..1114
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 1138..1140
FT /evidence="ECO:0007829|PDB:6W6W"
FT HELIX 1141..1145
FT /evidence="ECO:0007829|PDB:6W6W"
FT TURN 1149..1151
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1154..1161
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1175..1177
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1188..1190
FT /evidence="ECO:0007829|PDB:6W6W"
FT STRAND 1195..1203
FT /evidence="ECO:0007829|PDB:6W6W"
SQ SEQUENCE 1217 AA; 134609 MW; EF6B3985C72FDA6E CRC64;
MAAGRAQVPS SEQAWLEDAQ VFIQKTLCPA VKEPNVQLTP LVIDCVKTVW LSQGRNQGST
LPLSYSFVSV QDLKTHQRLP CCSHLSWSSS AYQAWAQEAG PNGNPLPREQ LLLLGTLTDL
SADLEQECRN GSLYVRDNTG VLSCELIDLD LSWLGHLFLF PRWSYLPPAR WNSSGEGHLE
LWDAPVPVFP LTISPGPVTP IPVLYPESAS CLLRLRNKLR GVQRNLAGSL VRLSALVKSK
QKAYFILSLG RSHPAVTHVS IIVQVPAQLV WHRALRPGTA YVLTELRVSK IRGQRQHVWM
TSQSSRLLLL KPECVQELEL ELEGPLLEAD PKPLPMPSNS EDKKDPESLV RYSRLLSYSG
AVTGVLNEPA GLYELDGQLG LCLAYQQFRG LRRVMRPGVC LQLQDVHLLQ SVGGGTRRPV
LAPCLRGAVL LQSFSRQKPG AHSSRQAYGA SLYEQLVWER QLGLPLYLWA TKALEELACK
LCPHVLRHHQ FLQHSSPGSP SLGLQLLAPT LDLLAPPGSP VRNAHNEILE EPHHCPLQKY
TRLQTPSSFP TLATLKEEGQ RKAWASFDPK ALLPLPEASY LPSCQLNRRL AWSWLCLLPS
AFCPAQVLLG VLVASSHKGC LQLRDQSGSL PCLLLAKHSQ PLSDPRLIGC LVRAERFQLI
VERDVRSSFP SWKELSMPGF IQKQQARVYV QFFLADALIL PVPRPCLHSA TPSTPQTDPT
GPEGPHLGQS RLFLLCHKEA LMKRNFCVPP GASPEVPKPA LSFYVLGSWL GGTQRKEGTG
WGLPEPQGND DNDQKVHLIF FGSSVRWFEF LHPGQVYRLI APGPATPMLF EKDGSSCISR
RPLELAGCAS CLTVQDNWTL ELESSQDIQD VLDANKSLPE SSLTDLLSDN FTDSLVSFSA
EILSRTLCEP LVASLWMKLG NTGAMRRCVK LTVALETAEC EFPPHLDVYI EDPHLPPSLG
LLPGARVHFS QLEKRVSRSH NVYCCFRSST YVQVLSFPPE TTISIPLPHI YLAELLQGGQ
SPFQATASCH IVSVFSLQLF WVCAYCTSIC RQGKCTRLGS TCPTQTAISQ AIIRLLVEDG
TAEAVVTCRN HHVAAALGLC PREWASLLDF VQVPGRVVLQ FAGPGAQLES SARVDEPMTM
FLWTLCTSPS VLRPIVLSFE LERKPSKIVP LEPPRLQRFQ CGELPFLTHV NPRLRLSCLS
IRESEYSSSL GILASSC
