CIP2A_HUMAN
ID CIP2A_HUMAN Reviewed; 905 AA.
AC Q8TCG1; A1L4J7; B9EGC3; Q6P4G6; Q8WVP8; Q96PI2; Q9H9C6; Q9P204;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein CIP2A {ECO:0000305};
DE AltName: Full=Cancerous inhibitor of PP2A {ECO:0000303|PubMed:17632056};
DE AltName: Full=p90 autoantigen {ECO:0000303|PubMed:12118381};
GN Name=CIP2A {ECO:0000312|HGNC:HGNC:29302}; Synonyms=KIAA1524;
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), SUBCELLULAR LOCATION, PRESENCE OF
RP AUTOANTIBODIES, AND TISSUE SPECIFICITY.
RX PubMed=12118381; DOI=10.1038/sj.onc.1205625;
RA Soo Hoo L., Zhang J.Y., Chan E.K.L.;
RT "Cloning and characterization of a novel 90 kDa 'companion' auto-antigen of
RT p62 overexpressed in cancer.";
RL Oncogene 21:5006-5015(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, Mammary gland, and Uterus;
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] (ISOFORM 1).
RC TISSUE=Melanoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 375-905.
RC TISSUE=Teratocarcinoma;
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 [7]
RP PRESENCE OF AUTOANTIBODIES.
RX PubMed=15538718; DOI=10.1002/pros.20181;
RA Shi F.D., Zhang J.Y., Liu D., Rearden A., Elliot M., Nachtsheim D.,
RA Daniels T., Casiano C.A., Heeb M.J., Chan E.K.L., Tan E.M.;
RT "Preferential humoral immune response in prostate cancer to cellular
RT proteins p90 and p62 in a panel of tumor-associated antigens.";
RL Prostate 63:252-258(2005).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH MYC.
RX PubMed=17632056; DOI=10.1016/j.cell.2007.04.044;
RA Junttila M.R., Puustinen P., Niemelae M., Ahola R., Arnold H.,
RA Boettzauw T., Ala-Aho R., Nielsen C., Ivaska J., Taya Y., Lu S.-L., Lin S.,
RA Chan E.K.L., Wang X.-J., Grenman R., Kast J., Kallunki T., Sears R.,
RA Kaehaeri V.-M., Westermarck J.;
RT "CIP2A inhibits PP2A in human malignancies.";
RL Cell 130:51-62(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573 AND SER-904, AND
RP IDENTIFICATION BY 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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-560, SUBUNIT, INTERACTION WITH
RP PPP2R5C AND PPP2R1A, AND MUTAGENESIS OF ASN-230; ARG-522 AND LEU-533.
RX PubMed=28174209; DOI=10.15252/embr.201642788;
RA Wang J., Okkeri J., Pavic K., Wang Z., Kauko O., Halonen T., Sarek G.,
RA Ojala P.M., Rao Z., Xu W., Westermarck J.;
RT "Oncoprotein CIP2A is stabilized via interaction with tumor suppressor
RT PP2A/B56.";
RL EMBO Rep. 18:437-450(2017).
CC -!- FUNCTION: Oncoprotein that inhibits PP2A and stabilizes MYC in human
CC malignancies. Promotes anchorage-independent cell growth and tumor
CC formation. {ECO:0000269|PubMed:17632056}.
CC -!- SUBUNIT: Homodimer (PubMed:28174209). Interacts with MYC
CC (PubMed:17632056). Interacts with PPP2R5C; this interaction stabilizes
CC CIP2A (PubMed:28174209). Interacts with PPP2R1A; this interaction
CC stabilizes CIP2A (PubMed:28174209). {ECO:0000269|PubMed:17632056,
CC ECO:0000269|PubMed:28174209}.
CC -!- INTERACTION:
CC Q8TCG1; P01106: MYC; NbExp=2; IntAct=EBI-1379376, EBI-447544;
CC Q8TCG1; P30153: PPP2R1A; NbExp=4; IntAct=EBI-1379376, EBI-302388;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:12118381}.
CC Note=Slightly concentrates in the perinuclear region (PubMed:12118381).
CC {ECO:0000269|PubMed:12118381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TCG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCG1-2; Sequence=VSP_025336;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in most of the tissues.
CC Overexpressed in head-and-neck squamous cell carcinomas (HNSCC).
CC Present in liver cancer cells (at protein level).
CC {ECO:0000269|PubMed:12118381, ECO:0000269|PubMed:17632056}.
CC -!- MISCELLANEOUS: Antibodies against CIP2A are present in sera from many
CC patients with gastric or prostate cancer, suggesting that it may act as
CC a marker for such cancers. {ECO:0000269|PubMed:12118381,
CC ECO:0000269|PubMed:15538718}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63433.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA96048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KIAA1524ID44402ch3q13.html";
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DR EMBL; AF334474; AAL11632.1; -; mRNA.
DR EMBL; AB040957; BAA96048.1; ALT_INIT; mRNA.
DR EMBL; AL713689; CAD28489.1; -; mRNA.
DR EMBL; BC017659; AAH17659.1; -; mRNA.
DR EMBL; BC063433; AAH63433.1; ALT_INIT; mRNA.
DR EMBL; BC130564; AAI30565.1; -; mRNA.
DR EMBL; BC136371; AAI36372.1; -; mRNA.
DR EMBL; AK022912; BAB14305.1; ALT_INIT; mRNA.
DR CCDS; CCDS33812.1; -. [Q8TCG1-1]
DR RefSeq; NP_065941.2; NM_020890.2. [Q8TCG1-1]
DR RefSeq; XP_006713780.1; XM_006713717.2. [Q8TCG1-2]
DR RefSeq; XP_011511358.1; XM_011513056.1. [Q8TCG1-2]
DR PDB; 5UFL; X-ray; 3.00 A; A/B=1-560.
DR PDBsum; 5UFL; -.
DR AlphaFoldDB; Q8TCG1; -.
DR SMR; Q8TCG1; -.
DR BioGRID; 121687; 136.
DR IntAct; Q8TCG1; 44.
DR MINT; Q8TCG1; -.
DR STRING; 9606.ENSP00000295746; -.
DR ChEMBL; CHEMBL2146355; -.
DR GlyGen; Q8TCG1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TCG1; -.
DR PhosphoSitePlus; Q8TCG1; -.
DR BioMuta; CIP2A; -.
DR DMDM; 147647143; -.
DR EPD; Q8TCG1; -.
DR jPOST; Q8TCG1; -.
DR MassIVE; Q8TCG1; -.
DR MaxQB; Q8TCG1; -.
DR PaxDb; Q8TCG1; -.
DR PeptideAtlas; Q8TCG1; -.
DR PRIDE; Q8TCG1; -.
DR ProteomicsDB; 74132; -. [Q8TCG1-1]
DR ProteomicsDB; 74133; -. [Q8TCG1-2]
DR Antibodypedia; 32380; 270 antibodies from 22 providers.
DR DNASU; 57650; -.
DR Ensembl; ENST00000295746.13; ENSP00000295746.7; ENSG00000163507.15. [Q8TCG1-1]
DR Ensembl; ENST00000491772.5; ENSP00000419487.1; ENSG00000163507.15. [Q8TCG1-2]
DR GeneID; 57650; -.
DR KEGG; hsa:57650; -.
DR MANE-Select; ENST00000295746.13; ENSP00000295746.7; NM_020890.3; NP_065941.2.
DR UCSC; uc003dxb.5; human. [Q8TCG1-1]
DR CTD; 57650; -.
DR DisGeNET; 57650; -.
DR GeneCards; CIP2A; -.
DR HGNC; HGNC:29302; CIP2A.
DR HPA; ENSG00000163507; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 610643; gene.
DR neXtProt; NX_Q8TCG1; -.
DR OpenTargets; ENSG00000163507; -.
DR PharmGKB; PA134887850; -.
DR VEuPathDB; HostDB:ENSG00000163507; -.
DR eggNOG; ENOG502QTAP; Eukaryota.
DR GeneTree; ENSGT00940000153251; -.
DR HOGENOM; CLU_014754_0_0_1; -.
DR InParanoid; Q8TCG1; -.
DR OMA; AYKMLII; -.
DR OrthoDB; 188665at2759; -.
DR PhylomeDB; Q8TCG1; -.
DR TreeFam; TF328534; -.
DR PathwayCommons; Q8TCG1; -.
DR SignaLink; Q8TCG1; -.
DR BioGRID-ORCS; 57650; 120 hits in 1084 CRISPR screens.
DR ChiTaRS; KIAA1524; human.
DR GeneWiki; KIAA1524; -.
DR GenomeRNAi; 57650; -.
DR Pharos; Q8TCG1; Tbio.
DR PRO; PR:Q8TCG1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8TCG1; protein.
DR Bgee; ENSG00000163507; Expressed in ventricular zone and 106 other tissues.
DR ExpressionAtlas; Q8TCG1; baseline and differential.
DR Genevisible; Q8TCG1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR042510; CIP2A.
DR PANTHER; PTHR23161; PTHR23161; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..905
FT /note="Protein CIP2A"
FT /id="PRO_0000287141"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 159..245
FT /note="Required for interaction with PPP2R5C"
FT /evidence="ECO:0000269|PubMed:28174209"
FT REGION 388..558
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:28174209"
FT COILED 637..883
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_025336"
FT VARIANT 126
FT /note="K -> R (in dbSNP:rs7648496)"
FT /id="VAR_046939"
FT VARIANT 229
FT /note="R -> Q (in dbSNP:rs2278911)"
FT /id="VAR_046940"
FT VARIANT 409
FT /note="T -> I (in dbSNP:rs9856308)"
FT /id="VAR_046941"
FT VARIANT 447
FT /note="T -> A (in dbSNP:rs34944683)"
FT /id="VAR_046942"
FT VARIANT 494
FT /note="P -> L (in dbSNP:rs13083928)"
FT /id="VAR_046943"
FT VARIANT 572
FT /note="S -> A (in dbSNP:rs34172460)"
FT /id="VAR_046944"
FT VARIANT 680
FT /note="R -> T (in dbSNP:rs6777766)"
FT /id="VAR_046945"
FT VARIANT 759
FT /note="I -> V (in dbSNP:rs13071874)"
FT /id="VAR_046946"
FT MUTAGEN 230
FT /note="N->E: Reduces binding to PPP2R5C."
FT /evidence="ECO:0000269|PubMed:28174209"
FT MUTAGEN 522
FT /note="R->D: Decreases homodimerization. Reduces binding to
FT PPP2R5C. Decreases protein level."
FT /evidence="ECO:0000269|PubMed:28174209"
FT MUTAGEN 533
FT /note="L->E: Decreases homodimerization. Reduces binding to
FT PPP2R5C. Decreases protein level."
FT /evidence="ECO:0000269|PubMed:28174209"
FT CONFLICT 412..415
FT /note="KCER -> NVKG (in Ref. 3; CAD28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="A -> S (in Ref. 1; AAL11632)"
FT /evidence="ECO:0000305"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:5UFL"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:5UFL"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:5UFL"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 293..307
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 358..374
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 379..394
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 406..426
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 442..456
FT /evidence="ECO:0007829|PDB:5UFL"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 470..489
FT /evidence="ECO:0007829|PDB:5UFL"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 496..504
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 510..517
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 522..535
FT /evidence="ECO:0007829|PDB:5UFL"
FT HELIX 543..558
FT /evidence="ECO:0007829|PDB:5UFL"
SQ SEQUENCE 905 AA; 102185 MW; DAB9CCC03BCEA304 CRC64;
MDSTACLKSL LLTVSQYKAV KSEANATQLL RHLEVISGQK LTRLFTSNQI LTSECLSCLV
ELLEDPNISA SLILSIIGLL SQLAVDIETR DCLQNTYNLN SVLAGVVCRS SHTDSVFLQC
IQLLQKLTYN VKIFYSGANI DELITFLIDH IQSSEDELKM PCLGLLANLC RHNLSVQTHI
KTLSNVKSFY RTLITLLAHS SLTVVVFALS ILSSLTLNEE VGEKLFHARN IHQTFQLIFN
ILINGDGTLT RKYSVDLLMD LLKNPKIADY LTRYEHFSSC LHQVLGLLNG KDPDSSSKVL
ELLLAFCSVT QLRHMLTQMM FEQSPPGSAT LGSHTKCLEP TVALLRWLSQ PLDGSENCSV
LALELFKEIF EDVIDAANCS SADRFVTLLL PTILDQLQFT EQNLDEALTR KKCERIAKAI
EVLLTLCGDD TLKMHIAKIL TTVKCTTLIE QQFTYGKIDL GFGTKVADSE LCKLAADVIL
KTLDLINKLK PLVPGMEVSF YKILQDPRLI TPLAFALTSD NREQVQSGLR ILLEAAPLPD
FPALVLGESI AANNAYRQQE TEHIPRKMPW QSSNHSFPTS IKCLTPHLKD GVPGLNIEEL
IEKLQSGMVV KDQICDVRIS DIMDVYEMKL STLASKESRL QDLLETKALA LAQADRLIAQ
HRCQRTQAET EARTLASMLR EVERKNEELS VLLKAQQVES ERAQSDIEHL FQHNRKLESV
AEEHEILTKS YMELLQRNES TEKKNKDLQI TCDSLNKQIE TVKKLNESLK EQNEKSIAQL
IEKEEQRKEV QNQLVDREHK LANLHQKTKV QEEKIKTLQK EREDKEETID ILRKELSRTE
QIRKELSIKA SSLEVQKAQL EGRLEEKESL VKLQQEELNK HSHMIAMIHS LSGGKINPET
VNLSI
