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CNO10_HUMAN
ID   CNO10_HUMAN             Reviewed;         744 AA.
AC   Q9H9A5; B7Z7L1; F8WAF2; Q9BU30; Q9H5J7; Q9H8X1; Q9H9W0; Q9HAH3; Q9UFJ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=CCR4-NOT transcription complex subunit 10;
GN   Name=CNOT10;
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; 5 AND 6), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 85-744 (ISOFORM 4), AND VARIANT SER-348.
RC   TISSUE=Embryo, 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=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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] (ISOFORMS 1 AND 3), AND VARIANT
RP   SER-736.
RC   TISSUE=Skin;
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 [LARGE SCALE MRNA] OF 482-744 (ISOFORM 1).
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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [7]
RP   IDENTIFICATION IN THE CCR4-NOT COMPLEX, AND COMPOSITION OF THE CCR4-NOT
RP   COMPLEX.
RX   PubMed=19558367; DOI=10.1042/bj20090500;
RA   Lau N.C., Kolkman A., van Schaik F.M., Mulder K.W., Pijnappel W.W.,
RA   Heck A.J., Timmers H.T.;
RT   "Human Ccr4-Not complexes contain variable deadenylase subunits.";
RL   Biochem. J. 422:443-453(2009).
RN   [8]
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   [9]
RP   IDENTIFICATION IN THE CCR4-NOT COMPLEX.
RX   PubMed=23232451; DOI=10.4161/rna.23065;
RA   Mauxion F., Preve B., Seraphin B.;
RT   "C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex.";
RL   RNA Biol. 10:267-276(2013).
RN   [10]
RP   FUNCTION.
RX   PubMed=23221646; DOI=10.1093/nar/gks1133;
RA   Farber V., Erben E., Sharma S., Stoecklin G., Clayton C.;
RT   "Trypanosome CNOT10 is essential for the integrity of the NOT deadenylase
RT   complex and for degradation of many mRNAs.";
RL   Nucleic Acids Res. 41:1211-1222(2013).
RN   [11]
RP   INTERACTION WITH CNOT11.
RX   PubMed=23303381; DOI=10.4161/rna.23018;
RA   Bawankar P., Loh B., Wohlbold L., Schmidt S., Izaurralde E.;
RT   "NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex
RT   that docks onto the NOT1 N-terminal domain.";
RL   RNA Biol. 10:228-244(2013).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Component of the CCR4-NOT complex which is one of the major
CC       cellular mRNA deadenylases and is linked to various cellular processes
CC       including bulk mRNA degradation, miRNA-mediated repression,
CC       translational repression during translational initiation and general
CC       transcription regulation. Additional complex functions may be a
CC       consequence of its influence on mRNA expression. Is not required for
CC       association of CNOT7 to the CCR4-NOT complex.
CC       {ECO:0000269|PubMed:23221646}.
CC   -!- SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to
CC       exist that differ in the participation of probably mutually exclusive
CC       catalytic subunits. CNOT10 and CNOT11 form a subcomplex docked to the
CC       CNOT1 scaffold. {ECO:0000269|PubMed:19558367,
CC       ECO:0000269|PubMed:23232451}.
CC   -!- INTERACTION:
CC       Q9H9A5; Q9UKZ1: CNOT11; NbExp=4; IntAct=EBI-1054261, EBI-2562014;
CC       Q9H9A5; P42858: HTT; NbExp=4; IntAct=EBI-1054261, EBI-466029;
CC       Q9H9A5; Q9HCJ0: TNRC6C; NbExp=10; IntAct=EBI-1054261, EBI-6507625;
CC       Q9H9A5-3; P42858: HTT; NbExp=3; IntAct=EBI-25957177, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q9H9A5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H9A5-2; Sequence=VSP_030312;
CC       Name=3;
CC         IsoId=Q9H9A5-3; Sequence=VSP_030313;
CC       Name=4;
CC         IsoId=Q9H9A5-4; Sequence=VSP_030313, VSP_030314;
CC       Name=5;
CC         IsoId=Q9H9A5-5; Sequence=VSP_030311;
CC       Name=6;
CC         IsoId=Q9H9A5-6; Sequence=VSP_045557;
CC   -!- SIMILARITY: Belongs to the CNOT10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB13876.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK021695; BAB13876.1; ALT_INIT; mRNA.
DR   EMBL; AK022576; BAB14108.1; -; mRNA.
DR   EMBL; AK022952; BAB14327.1; -; mRNA.
DR   EMBL; AK023227; BAB14478.1; -; mRNA.
DR   EMBL; AK027026; BAB15629.1; -; mRNA.
DR   EMBL; AK302196; BAH13647.1; -; mRNA.
DR   EMBL; AC138972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC139452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64435.1; -; Genomic_DNA.
DR   EMBL; BC002928; AAH02928.1; -; mRNA.
DR   EMBL; BC002931; AAH02931.1; -; mRNA.
DR   EMBL; AL117639; CAB56027.2; -; mRNA.
DR   CCDS; CCDS2655.1; -. [Q9H9A5-1]
DR   CCDS; CCDS58821.1; -. [Q9H9A5-3]
DR   CCDS; CCDS58822.1; -. [Q9H9A5-6]
DR   RefSeq; NP_001243670.1; NM_001256741.1. [Q9H9A5-3]
DR   RefSeq; NP_001243671.1; NM_001256742.1. [Q9H9A5-6]
DR   RefSeq; NP_056257.1; NM_015442.2. [Q9H9A5-1]
DR   AlphaFoldDB; Q9H9A5; -.
DR   BioGRID; 117411; 123.
DR   ComplexPortal; CPX-2522; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT7 variant.
DR   ComplexPortal; CPX-2535; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT8 variant.
DR   ComplexPortal; CPX-2849; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT8 variant.
DR   ComplexPortal; CPX-707; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT7 variant.
DR   CORUM; Q9H9A5; -.
DR   DIP; DIP-46839N; -.
DR   IntAct; Q9H9A5; 47.
DR   MINT; Q9H9A5; -.
DR   STRING; 9606.ENSP00000399862; -.
DR   ChEMBL; CHEMBL4105878; -.
DR   GlyGen; Q9H9A5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H9A5; -.
DR   PhosphoSitePlus; Q9H9A5; -.
DR   BioMuta; CNOT10; -.
DR   DMDM; 74733982; -.
DR   EPD; Q9H9A5; -.
DR   jPOST; Q9H9A5; -.
DR   MassIVE; Q9H9A5; -.
DR   MaxQB; Q9H9A5; -.
DR   PaxDb; Q9H9A5; -.
DR   PeptideAtlas; Q9H9A5; -.
DR   PRIDE; Q9H9A5; -.
DR   ProteomicsDB; 30485; -.
DR   ProteomicsDB; 81300; -. [Q9H9A5-1]
DR   ProteomicsDB; 81301; -. [Q9H9A5-2]
DR   ProteomicsDB; 81302; -. [Q9H9A5-3]
DR   ProteomicsDB; 81303; -. [Q9H9A5-4]
DR   ProteomicsDB; 81304; -. [Q9H9A5-5]
DR   Antibodypedia; 27780; 88 antibodies from 22 providers.
DR   DNASU; 25904; -.
DR   Ensembl; ENST00000328834.10; ENSP00000330060.5; ENSG00000182973.20. [Q9H9A5-1]
DR   Ensembl; ENST00000331889.10; ENSP00000329376.6; ENSG00000182973.20. [Q9H9A5-3]
DR   Ensembl; ENST00000454516.7; ENSP00000399862.2; ENSG00000182973.20. [Q9H9A5-6]
DR   GeneID; 25904; -.
DR   KEGG; hsa:25904; -.
DR   MANE-Select; ENST00000328834.10; ENSP00000330060.5; NM_015442.3; NP_056257.1.
DR   UCSC; uc003cfc.2; human. [Q9H9A5-1]
DR   CTD; 25904; -.
DR   GeneCards; CNOT10; -.
DR   HGNC; HGNC:23817; CNOT10.
DR   HPA; ENSG00000182973; Low tissue specificity.
DR   neXtProt; NX_Q9H9A5; -.
DR   PharmGKB; PA134862503; -.
DR   VEuPathDB; HostDB:ENSG00000182973; -.
DR   eggNOG; KOG2471; Eukaryota.
DR   GeneTree; ENSGT00390000001827; -.
DR   HOGENOM; CLU_013100_0_0_1; -.
DR   InParanoid; Q9H9A5; -.
DR   OMA; VWCFSKA; -.
DR   OrthoDB; 249353at2759; -.
DR   PhylomeDB; Q9H9A5; -.
DR   TreeFam; TF323368; -.
DR   PathwayCommons; Q9H9A5; -.
DR   Reactome; R-HSA-429947; Deadenylation of mRNA.
DR   Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR   SignaLink; Q9H9A5; -.
DR   SIGNOR; Q9H9A5; -.
DR   BioGRID-ORCS; 25904; 43 hits in 1089 CRISPR screens.
DR   ChiTaRS; CNOT10; human.
DR   GenomeRNAi; 25904; -.
DR   Pharos; Q9H9A5; Tdark.
DR   PRO; PR:Q9H9A5; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9H9A5; protein.
DR   Bgee; ENSG00000182973; Expressed in right testis and 132 other tissues.
DR   ExpressionAtlas; Q9H9A5; baseline and differential.
DR   Genevisible; Q9H9A5; HS.
DR   GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IC:ComplexPortal.
DR   Gene3D; 1.25.40.10; -; 2.
DR   InterPro; IPR039740; CNOT10.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR12979; PTHR12979; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW   Reference proteome; RNA-mediated gene silencing; Transcription;
KW   Transcription regulation; Translation regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..744
FT                   /note="CCR4-NOT transcription complex subunit 10"
FT                   /id="PRO_0000314579"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          74..107
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        183..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   VAR_SEQ         1..293
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030311"
FT   VAR_SEQ         1..7
FT                   /note="MAADKPA -> MKSIGVKTVKVCGSKSSVRIEGQPCSLGQSRRKVKLMGERS
FT                   YTLSIGNGDYFWANKEMLWDYVQTLS (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045557"
FT   VAR_SEQ         144
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030312"
FT   VAR_SEQ         505..532
FT                   /note="SSKSHDGDKFIPAPPSSPLRKQELENLK -> R (in isoform 3 and
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030313"
FT   VAR_SEQ         556..577
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030314"
FT   VARIANT         348
FT                   /note="T -> S (in dbSNP:rs11558687)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_053982"
FT   VARIANT         736
FT                   /note="P -> S (in dbSNP:rs17849684)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_037957"
FT   CONFLICT        5
FT                   /note="K -> R (in Ref. 1; BAB14108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="C -> R (in Ref. 1; BAB14478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="V -> M (in Ref. 1; BAB13876)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        478
FT                   /note="D -> G (in Ref. 1; BAB14108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="H -> Y (in Ref. 1; BAB14108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        518
FT                   /note="P -> L (in Ref. 1; BAH13647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        622
FT                   /note="A -> T (in Ref. 1; BAB14478)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   744 AA;  82310 MW;  BA1984B71F0A1E7A CRC64;
     MAADKPADQG AEKHEGTGQS SGITDQEKEL STNAFQAFTS GNYDACLQHL ACLQDINKDD
     YKIILNTAVA EFFKSNQTTT DNLRQTLNQL KNQVHSAVEE MDGLDDVENS MLYYNQAVIL
     YHLRQYTEAI SVGEKLYQFI EPFEEKFAQA VCFLLVDLYI LTYQAEKALH LLAVLEKMIS
     QGNNNKNGKN ETGNNNNKDG SNHKAESGAL IEAAKSKIHQ YKVRAYIQMK SLKACKREIK
     SVMNTAGNSA PSLFLKSNFE YLRGNYRKAV KLLNSSNIAE HPGFMKTGEC LRCMFWNNLG
     CIHFAMSKHN LGIFYFKKAL QENDNVCAQL SAGSTDPGKK FSGRPMCTLL TNKRYELLYN
     CGIQLLHIGR PLAAFECLIE AVQVYHANPR LWLRLAECCI AANKGTSEQE TKGLPSKKGI
     VQSIVGQGYH RKIVLASQSI QNTVYNDGQS SAIPVASMEF AAICLRNALL LLPEEQQDPK
     QENGAKNSNQ LGGNTESSES SETCSSKSHD GDKFIPAPPS SPLRKQELEN LKCSILACSA
     YVALALGDNL MALNHADKLL QQPKLSGSLK FLGHLYAAEA LISLDRISDA ITHLNPENVT
     DVSLGISSNE QDQGSDKGEN EAMESSGKRA PQCYPSSVNS ARTVMLFNLG SAYCLRSEYD
     KARKCLHQAA SMIHPKEVPP EAILLAVYLE LQNGNTQLAL QIIKRNQLLP AVKTHSEVRK
     KPVFQPVHPI QPIQMPAFTT VQRK
 
 
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