Z3H7B_HUMAN
ID Z3H7B_HUMAN Reviewed; 977 AA.
AC Q9UGR2; A7YY88; B2RCA4; Q5TFX9; Q8TBT9; Q9H8B6; Q9UGQ9; Q9UGR0; Q9UGR1;
AC Q9UK03; Q9UPW9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Zinc finger CCCH domain-containing protein 7B;
DE AltName: Full=Rotavirus 'X'-associated non-structural protein;
DE Short=RoXaN;
GN Name=ZC3H7B; Synonyms=KIAA1031;
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=Trachea;
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=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-764, AND INTERACTION WITH ROTAVIRUS A NSP3
RP (MICROBIAL INFECTION).
RA Lindenbaum P.;
RT "RoXaN: a tetratricopeptide cellular protein interacting with rotavirus
RT non-structural protein NSP3.";
RL Thesis (2000), University of Paris XI, France.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-977.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [6]
RP INTERACTION WITH ROTAVIRUS A NSP3 (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP 241-ASP--SER-243 AND 252-LEU--ASP-254.
RX PubMed=15047801; DOI=10.1128/jvi.78.8.3851-3862.2004;
RA Vitour D., Lindenbaum P., Vende P., Becker M.M., Poncet D.;
RT "RoXaN, a novel cellular protein containing TPR, LD, and zinc finger
RT motifs, forms a ternary complex with eukaryotic initiation factor 4G and
RT rotavirus NSP3.";
RL J. Virol. 78:3851-3862(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ROTAVIRUS A NSP3 (MICROBIAL
RP INFECTION).
RX PubMed=18799579; DOI=10.1128/jvi.00872-08;
RA Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C.,
RA Bolte S., Arold S.T., Poncet D.;
RT "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus
RT infection involves the interaction of NSP3 with eIF4G and RoXaN.";
RL J. Virol. 82:11283-11293(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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 [10]
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 [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP 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 [14]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
CC -!- FUNCTION: May be a specific regulator of miRNA biogenesis. Binds to
CC microRNAs MIR7-1, MIR16-2 and MIR29A hairpins recognizing the
CC 'ATA(A/T)' motif in the apical loop. {ECO:0000269|PubMed:28431233}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via LD motif) with rotavirus
CC A NSP3 (via the coiled-coil region). {ECO:0000269|PubMed:15047801,
CC ECO:0000269|Ref.4}.
CC -!- INTERACTION:
CC Q9UGR2; Q00721; Xeno; NbExp=6; IntAct=EBI-948845, EBI-1263962;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18799579}.
CC Note=Nuclear localization seems to be depleted upon rotavirus A
CC infection.
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DR EMBL; AK315009; BAG37501.1; -; mRNA.
DR EMBL; AL035659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024313; AAH24313.2; -; mRNA.
DR EMBL; BC152558; AAI52559.1; -; mRNA.
DR EMBL; AF188530; AAF05541.1; -; mRNA.
DR EMBL; AB028954; BAA82983.1; -; mRNA.
DR CCDS; CCDS14013.1; -.
DR RefSeq; NP_060060.3; NM_017590.5.
DR AlphaFoldDB; Q9UGR2; -.
DR SMR; Q9UGR2; -.
DR BioGRID; 116866; 34.
DR IntAct; Q9UGR2; 18.
DR MINT; Q9UGR2; -.
DR STRING; 9606.ENSP00000345793; -.
DR iPTMnet; Q9UGR2; -.
DR PhosphoSitePlus; Q9UGR2; -.
DR BioMuta; ZC3H7B; -.
DR DMDM; 20455239; -.
DR EPD; Q9UGR2; -.
DR jPOST; Q9UGR2; -.
DR MassIVE; Q9UGR2; -.
DR MaxQB; Q9UGR2; -.
DR PaxDb; Q9UGR2; -.
DR PeptideAtlas; Q9UGR2; -.
DR PRIDE; Q9UGR2; -.
DR Antibodypedia; 203; 121 antibodies from 27 providers.
DR DNASU; 23264; -.
DR Ensembl; ENST00000352645.5; ENSP00000345793.4; ENSG00000100403.12.
DR GeneID; 23264; -.
DR KEGG; hsa:23264; -.
DR MANE-Select; ENST00000352645.5; ENSP00000345793.4; NM_017590.6; NP_060060.3.
DR UCSC; uc003azw.5; human.
DR CTD; 23264; -.
DR DisGeNET; 23264; -.
DR GeneCards; ZC3H7B; -.
DR HGNC; HGNC:30869; ZC3H7B.
DR HPA; ENSG00000100403; Low tissue specificity.
DR MIM; 618206; gene.
DR neXtProt; NX_Q9UGR2; -.
DR OpenTargets; ENSG00000100403; -.
DR PharmGKB; PA142670533; -.
DR VEuPathDB; HostDB:ENSG00000100403; -.
DR eggNOG; ENOG502QVIS; Eukaryota.
DR GeneTree; ENSGT00390000018542; -.
DR HOGENOM; CLU_012672_0_0_1; -.
DR InParanoid; Q9UGR2; -.
DR OMA; RAMSFIQ; -.
DR OrthoDB; 369231at2759; -.
DR PhylomeDB; Q9UGR2; -.
DR TreeFam; TF329017; -.
DR PathwayCommons; Q9UGR2; -.
DR SignaLink; Q9UGR2; -.
DR BioGRID-ORCS; 23264; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; ZC3H7B; human.
DR GeneWiki; Roxan_(protein); -.
DR GenomeRNAi; 23264; -.
DR Pharos; Q9UGR2; Tbio.
DR PRO; PR:Q9UGR2; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UGR2; protein.
DR Bgee; ENSG00000100403; Expressed in endothelial cell and 203 other tissues.
DR Genevisible; Q9UGR2; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0035196; P:miRNA processing; IMP:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR039691; ZC3H7A/B.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14928; PTHR14928; 1.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00028; TPR; 2.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Zinc; Zinc-finger.
FT CHAIN 1..977
FT /note="Zinc finger CCCH domain-containing protein 7B"
FT /id="PRO_0000106322"
FT REPEAT 1..27
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 36..69
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 82..115
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT ZN_FING 484..508
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 616..638
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 754..782
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 842..866
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 886..914
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 365..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 248..256
FT /note="LD motif; interaction with NSP3"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 363
FT /note="D -> N (in dbSNP:rs9607793)"
FT /id="VAR_054313"
FT MUTAGEN 241..243
FT /note="DSS->AAA: Almost no effect on NSP3 binding."
FT /evidence="ECO:0000269|PubMed:15047801"
FT MUTAGEN 252..254
FT /note="LDD->AAA: Complete loss of NSP3 binding."
FT /evidence="ECO:0000269|PubMed:15047801"
FT CONFLICT 38..39
FT /note="NL -> LE (in Ref. 5; BAA82983)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="R -> K (in Ref. 4; AAF05541)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="G -> A (in Ref. 4; AAF05541)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="P -> T (in Ref. 3; AAI52559)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="G -> V (in Ref. 4; AAF05541)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="P -> T (in Ref. 3; AAI52559)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="S -> F (in Ref. 4; AAF05541)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="P -> L (in Ref. 3; AAI52559)"
FT /evidence="ECO:0000305"
FT CONFLICT 955
FT /note="E -> G (in Ref. 1; BAG37501 and 3; AAI52559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 109858 MW; BE3F8AEEC89D096D CRC64;
MERQKRKADI EKGLQFIQST LPLKQEEYEA FLLKLVQNLF AEGNDLFREK DYKQALVQYM
EGLNVADYAA SDQVALPREL LCKLHVNRAA CYFTMGLYEK ALEDSEKALG LDSESIRALF
RKARALNELG RHKEAYECSS RCSLALPHDE SVTQLGQELA QKLGLRVRKA YKRPQELETF
SLLSNGTAAG VADQGTSNGL GSIDDIETDC YVDPRGSPAL LPSTPTMPLF PHVLDLLAPL
DSSRTLPSTD SLDDFSDGDV FGPELDTLLD SLSLVQGGLS GSGVPSELPQ LIPVFPGGTP
LLPPVVGGSI PVSSPLPPAS FGLVMDPSKK LAASVLDALD PPGPTLDPLD LLPYSETRLD
ALDSFGSTRG SLDKPDSFME ETNSQDHRPP SGAQKPAPSP EPCMPNTALL IKNPLAATHE
FKQACQLCYP KTGPRAGDYT YREGLEHKCK RDILLGRLRS SEDQTWKRIR PRPTKTSFVG
SYYLCKDMIN KQDCKYGDNC TFAYHQEEID VWTEERKGTL NRDLLFDPLG GVKRGSLTIA
KLLKEHQGIF TFLCEICFDS KPRIISKGTK DSPSVCSNLA AKHSFYNNKC LVHIVRSTSL
KYSKIRQFQE HFQFDVCRHE VRYGCLREDS CHFAHSFIEL KVWLLQQYSG MTHEDIVQES
KKYWQQMEAH AGKASSSMGA PRTHGPSTFD LQMKFVCGQC WRNGQVVEPD KDLKYCSAKA
RHCWTKERRV LLVMSKAKRK WVSVRPLPSI RNFPQQYDLC IHAQNGRKCQ YVGNCSFAHS
PEERDMWTFM KENKILDMQQ TYDMWLKKHN PGKPGEGTPI SSREGEKQIQ MPTDYADIMM
GYHCWLCGKN SNSKKQWQQH IQSEKHKEKV FTSDSDASGW AFRFPMGEFR LCDRLQKGKA
CPDGDKCRCA HGQEELNEWL DRREVLKQKL AKARKDMLLC PRDDDFGKYN FLLQEDGDLA
GATPEAPAAA ATATTGE
