ZC11A_HUMAN
ID ZC11A_HUMAN Reviewed; 810 AA.
AC O75152; Q6AHY4; Q6AHY9; Q6AW79; Q6AWA1; Q6PJK4; Q86XZ7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Zinc finger CCCH domain-containing protein 11A;
GN Name=ZC3H11A; Synonyms=KIAA0663, ZC3HDC11A;
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].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal kidney, and Retina;
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 MRNA].
RC TISSUE=Kidney, and Placenta;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-132; SER-171;
RP SER-290 AND THR-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP 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 [10]
RP ASSOCIATION WITH THE TREX COMPLEX.
RX PubMed=20844015; DOI=10.1101/gad.1898610;
RA Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.;
RT "ATP is required for interactions between UAP56 and two conserved mRNA
RT export proteins, Aly and CIP29, to assemble the TREX complex.";
RL Genes Dev. 24:2043-2053(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-132, AND
RP IDENTIFICATION BY 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-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THOC2; DDX39B AND POLDIP3,
RP AND ASSOCIATION WITH THE TREX COMPLEX.
RX PubMed=22928037; DOI=10.1371/journal.pone.0043804;
RA Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.;
RT "The proteins PDIP3 and ZC11A associate with the human TREX complex in an
RT ATP-dependent manner and function in mRNA export.";
RL PLoS ONE 7:E43804-E43804(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-132; SER-171;
RP SER-290; THR-321 AND SER-370, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-290, AND
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).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-478, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-124; LYS-140; LYS-478
RP AND LYS-619, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND
RP INDUCTION BY HEAT SHOCK.
RX PubMed=29610341; DOI=10.1073/pnas.1722333115;
RA Younis S., Kamel W., Falkeborn T., Wang H., Yu D., Daniels R., Essand M.,
RA Hinkula J., Akusjaervi G., Andersson L.;
RT "Multiple nuclear-replicating viruses require the stress-induced protein
RT ZC3H11A for efficient growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E3808-E3816(2018).
CC -!- FUNCTION: RNA-binding protein that interacts with purine-rich sequences
CC and is involved in nuclear mRNA export; probably mediated by
CC association with the TREX complex. {ECO:0000269|PubMed:22928037,
CC ECO:0000269|PubMed:29610341}.
CC -!- FUNCTION: (Microbial infection) Plays a role in efficient growth of
CC several nuclear-replicating viruses such as HIV-1, influenza virus or
CC herpes simplex virus 1/HHV-1. Required for efficient viral mRNA Export.
CC {ECO:0000269|PubMed:29610341}.
CC -!- SUBUNIT: Interacts with THOC2, DDX39 and POLDIP3; the interactions are
CC ATP-dependent and indicative for an association with the TREX complex.
CC {ECO:0000269|PubMed:22928037}.
CC -!- INTERACTION:
CC O75152; Q08050: FOXM1; NbExp=2; IntAct=EBI-748480, EBI-866480;
CC O75152; P40692: MLH1; NbExp=7; IntAct=EBI-748480, EBI-744248;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29610341}.
CC -!- INDUCTION: By heat shock treatment. {ECO:0000269|PubMed:29610341}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31638.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH10553.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB014563; BAA31638.2; ALT_INIT; mRNA.
DR EMBL; CR627439; CAH10525.1; -; mRNA.
DR EMBL; CR627446; CAH10530.1; -; mRNA.
DR EMBL; BX648271; CAH10553.1; ALT_SEQ; mRNA.
DR EMBL; BX649148; CAH10566.1; -; mRNA.
DR EMBL; BC014268; AAH14268.1; -; mRNA.
DR CCDS; CCDS30978.1; -.
DR PIR; T00368; T00368.
DR RefSeq; NP_001306167.1; NM_001319238.1.
DR RefSeq; NP_001306168.1; NM_001319239.1.
DR RefSeq; NP_055642.3; NM_014827.5.
DR RefSeq; XP_005245700.1; XM_005245643.2.
DR RefSeq; XP_005245701.1; XM_005245644.3.
DR RefSeq; XP_006711736.1; XM_006711673.2.
DR RefSeq; XP_011508501.1; XM_011510199.1.
DR RefSeq; XP_011508502.1; XM_011510200.1.
DR RefSeq; XP_011508503.1; XM_011510201.1.
DR RefSeq; XP_011508504.1; XM_011510202.1.
DR RefSeq; XP_016858445.1; XM_017002956.1.
DR RefSeq; XP_016858446.1; XM_017002957.1.
DR RefSeq; XP_016858447.1; XM_017002958.1.
DR RefSeq; XP_016858448.1; XM_017002959.1.
DR AlphaFoldDB; O75152; -.
DR BioGRID; 115208; 154.
DR IntAct; O75152; 43.
DR MINT; O75152; -.
DR STRING; 9606.ENSP00000438527; -.
DR GlyGen; O75152; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75152; -.
DR MetOSite; O75152; -.
DR PhosphoSitePlus; O75152; -.
DR BioMuta; ZC3H11A; -.
DR CPTAC; CPTAC-1020; -.
DR EPD; O75152; -.
DR jPOST; O75152; -.
DR MassIVE; O75152; -.
DR MaxQB; O75152; -.
DR PaxDb; O75152; -.
DR PeptideAtlas; O75152; -.
DR PRIDE; O75152; -.
DR ProteomicsDB; 49818; -.
DR Antibodypedia; 34548; 153 antibodies from 25 providers.
DR DNASU; 9877; -.
DR Ensembl; ENST00000332127.8; ENSP00000333253.4; ENSG00000058673.17.
DR Ensembl; ENST00000367210.3; ENSP00000356179.1; ENSG00000058673.17.
DR Ensembl; ENST00000367212.7; ENSP00000356181.3; ENSG00000058673.17.
DR Ensembl; ENST00000367214.5; ENSP00000356183.1; ENSG00000058673.17.
DR Ensembl; ENST00000639812.1; ENSP00000491830.1; ENSG00000058673.17.
DR GeneID; 9877; -.
DR KEGG; hsa:9877; -.
DR MANE-Select; ENST00000367210.3; ENSP00000356179.1; NM_001376342.1; NP_001363271.1.
DR UCSC; uc001hac.4; human.
DR CTD; 9877; -.
DR DisGeNET; 9877; -.
DR GeneCards; ZC3H11A; -.
DR HGNC; HGNC:29093; ZC3H11A.
DR HPA; ENSG00000058673; Low tissue specificity.
DR MIM; 613513; gene.
DR neXtProt; NX_O75152; -.
DR OpenTargets; ENSG00000058673; -.
DR PharmGKB; PA142670535; -.
DR VEuPathDB; HostDB:ENSG00000058673; -.
DR eggNOG; KOG4791; Eukaryota.
DR GeneTree; ENSGT00920000149095; -.
DR HOGENOM; CLU_019514_1_0_1; -.
DR InParanoid; O75152; -.
DR OMA; VMKPAVQ; -.
DR OrthoDB; 265128at2759; -.
DR PhylomeDB; O75152; -.
DR TreeFam; TF335608; -.
DR PathwayCommons; O75152; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; O75152; -.
DR SIGNOR; O75152; -.
DR BioGRID-ORCS; 9877; 54 hits in 1081 CRISPR screens.
DR ChiTaRS; ZC3H11A; human.
DR GeneWiki; ZC3H11A; -.
DR GenomeRNAi; 9877; -.
DR Pharos; O75152; Tbio.
DR PRO; PR:O75152; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75152; protein.
DR Bgee; ENSG00000058673; Expressed in corpus callosum and 97 other tissues.
DR ExpressionAtlas; O75152; baseline and differential.
DR Genevisible; O75152; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:UniProtKB.
DR InterPro; IPR041686; Znf-CCCH_3.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF15663; zf-CCCH_3; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Metal-binding; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transport; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..810
FT /note="Zinc finger CCCH domain-containing protein 11A"
FT /id="PRO_0000213905"
FT ZN_FING 2..29
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 31..57
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 60..86
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 139..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..423
FT /evidence="ECO:0000255"
FT COMPBIAS 176..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 321
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 619
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 640
FT /note="T -> N (in dbSNP:rs11240604)"
FT /id="VAR_052967"
FT CONFLICT 80
FT /note="C -> Y (in Ref. 3; CAH10553)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="P -> L (in Ref. 3; CAH10530)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="L -> P (in Ref. 3; CAH10525)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="R -> G (in Ref. 3; CAH10530)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="V -> G (in Ref. 3; CAH10525)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="E -> K (in Ref. 3; CAH10525)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="S -> P (in Ref. 3; CAH10566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 89131 MW; 9048ABC7F4A372FB CRC64;
MPNQGEDCYF FFYSTCTKGD SCPFRHCEAA IGNETVCTLW QEGRCFRQVC RFRHMEIDKK
RSEIPCYWEN QPTGCQKLNC AFHHNRGRYV DGLFLPPSKT VLPTVPESPE EEVKASQLSV
QQNKLSVQSN PSPQLRSVMK VESSENVPSP THPPVVINAA DDDEDDDDQF SEEGDETKTP
TLQPTPEVHN GLRVTSVRKP AVNIKQGECL NFGIKTLEEI KSKKMKEKSK KQGEGSSGVS
SLLLHPEPVP GPEKENVRTV VRTVTLSTKQ GEEPLVRLSL TERLGKRKFS AGGDSDPPLK
RSLAQRLGKK VEAPETNIDK TPKKAQVSKS LKERLGMSAD PDNEDATDKV NKVGEIHVKT
LEEILLERAS QKRGELQTKL KTEGPSKTDD STSGARSSST IRIKTFSEVL AEKKHRQQEA
ERQKSKKDTT CIKLKIDSEI KKTVVLPPIV ASRGQSEEPA GKTKSMQEVH IKTLEEIKLE
KALRVQQSSE SSTSSPSQHE ATPGARRLLR ITKRTGMKEE KNLQEGNEVD SQSSIRTEAK
EASGETTGVD ITKIQVKRCE TMREKHMQKQ QEREKSVLTP LRGDVASCNT QVAEKPVLTA
VPGITRHLTK RLPTKSSQKV EVETSGIGDS LLNVKCAAQT LEKRGKAKPK VNVKPSVVKV
VSSPKLAPKR KAVEMHAAVI AAVKPLSSSS VLQEPPAKKA AVAVVPLVSE DKSVTVPEAE
NPRDSLVLPP TQSSSDSSPP EVSGPSSSQM SMKTRRLSSA STGKPPLSVE DDFEKLIWEI
SGGKLEAEID LDPGKDEDDL LLELSEMIDS
