REPI1_HUMAN
ID REPI1_HUMAN Reviewed; 567 AA.
AC Q9BWE0; C9J3L7; D3DWZ1; Q7LE03; Q9BUZ6; Q9NZH2; Q9UMP5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Replication initiator 1;
DE AltName: Full=60 kDa origin-specific DNA-binding protein;
DE AltName: Full=60 kDa replication initiation region protein;
DE AltName: Full=ATT-binding protein;
DE AltName: Full=DHFR oribeta-binding protein RIP60;
DE AltName: Full=Zinc finger protein 464;
GN Name=REPIN1; Synonyms=RIP60, ZNF464;
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], PROTEIN SEQUENCE OF 200-210 AND 501-518,
RP DNA-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=10606657; DOI=10.1093/nar/28.2.570;
RA Houchens C.R., Montigny W., Zeltser L., Dailey L., Gilbert J.M.,
RA Heintz N.H.;
RT "The dhfr oribeta-binding protein RIP60 contains 15 zinc fingers: DNA
RT binding and looping by the central three fingers and an associated proline-
RT rich region.";
RL Nucleic Acids Res. 28:570-581(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-14.
RC TISSUE=Cervix carcinoma;
RA Dobner T.G., Fischer M., Groitl P.;
RT "Cloning of a novel zinc finger protein.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-88.
RC TISSUE=Eye, and Muscle;
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 IDENTIFICATION IN A COMPLEX WITH RIP100, AND DNA-BINDING.
RX PubMed=2174103; DOI=10.1128/mcb.10.12.6225-6235.1990;
RA Dailey L., Caddle M.S., Heintz N., Heintz N.H.;
RT "Purification of RIP60 and RIP100, mammalian proteins with origin-specific
RT DNA-binding and ATP-dependent DNA helicase activities.";
RL Mol. Cell. Biol. 10:6225-6235(1990).
RN [7]
RP DNA-BINDING.
RX PubMed=2247056; DOI=10.1128/mcb.10.12.6236-6243.1990;
RA Caddle M.S., Dailey L., Heintz N.H.;
RT "RIP60, a mammalian origin-binding protein, enhances DNA bending near the
RT dihydrofolate reductase origin of replication.";
RL Mol. Cell. Biol. 10:6236-6243(1990).
RN [8]
RP SUBUNIT, IDENTIFICATION BY ELECTRON MICROSCOPY, AND DNA-BINDING.
RX PubMed=8355269; DOI=10.1006/jmbi.1993.1430;
RA Mastrangelo I.A., Held P.G., Dailey L., Wall J.S., Hough P.V., Heintz N.,
RA Heintz N.H.;
RT "RIP60 dimers and multiples of dimers assemble link structures at an origin
RT of bidirectional replication in the dihydrofolate reductase amplicon of
RT Chinese hamster ovary cells.";
RL J. Mol. Biol. 232:766-778(1993).
RN [9]
RP DNA-BINDING.
RX PubMed=11328883; DOI=10.1093/nar/29.9.1982;
RA Montigny W.J., Houchens C.R., Illenye S., Gilbert J., Coonrod E.,
RA Chang Y.-C., Heintz N.H.;
RT "Condensation by DNA looping facilitates transfer of large DNA molecules
RT into mammalian cells.";
RL Nucleic Acids Res. 29:1982-1988(2001).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33 AND LYS-276, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-30, 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).
CC -!- FUNCTION: Sequence-specific double-stranded DNA-binding protein
CC required for initiation of chromosomal DNA replication. Binds on 5'-
CC ATT-3' reiterated sequences downstream of the origin of bidirectional
CC replication (OBR) and a second, homologous ATT sequence of opposite
CC orientation situated within the OBR zone. Facilitates DNA bending.
CC -!- SUBUNIT: Homodimers and homomultimers. Found in a complex with RIP60
CC and RIP100. {ECO:0000269|PubMed:2174103, ECO:0000269|PubMed:8355269}.
CC -!- INTERACTION:
CC Q9BWE0-4; Q01105-2: SET; NbExp=3; IntAct=EBI-24236508, EBI-7481343;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10606657}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BWE0-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWE0-4; Sequence=VSP_054069;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00363.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAS00386.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB53100.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF201303; AAF26712.1; -; mRNA.
DR EMBL; AJ245553; CAB53100.1; ALT_FRAME; mRNA.
DR EMBL; AC005586; AAS00385.1; -; Genomic_DNA.
DR EMBL; AC005586; AAS00386.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471173; EAW54117.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54118.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54119.1; -; Genomic_DNA.
DR EMBL; BC000363; AAH00363.2; ALT_INIT; mRNA.
DR EMBL; BC001760; AAH01760.1; -; mRNA.
DR CCDS; CCDS43677.1; -. [Q9BWE0-3]
DR CCDS; CCDS47745.1; -. [Q9BWE0-4]
DR RefSeq; NP_001093165.1; NM_001099695.1. [Q9BWE0-4]
DR RefSeq; NP_001093166.1; NM_001099696.2. [Q9BWE0-3]
DR RefSeq; NP_037532.2; NM_013400.3. [Q9BWE0-3]
DR RefSeq; NP_055189.2; NM_014374.3.
DR RefSeq; XP_005250042.1; XM_005249985.1.
DR RefSeq; XP_006716010.1; XM_006715947.3. [Q9BWE0-4]
DR RefSeq; XP_006716011.1; XM_006715948.3.
DR RefSeq; XP_006716012.1; XM_006715949.3. [Q9BWE0-4]
DR RefSeq; XP_006716015.1; XM_006715952.2. [Q9BWE0-3]
DR RefSeq; XP_006716016.1; XM_006715953.2.
DR RefSeq; XP_011514414.1; XM_011516112.1.
DR RefSeq; XP_016867570.1; XM_017012081.1. [Q9BWE0-3]
DR RefSeq; XP_016867571.1; XM_017012082.1. [Q9BWE0-3]
DR AlphaFoldDB; Q9BWE0; -.
DR SMR; Q9BWE0; -.
DR BioGRID; 118927; 98.
DR IntAct; Q9BWE0; 25.
DR MINT; Q9BWE0; -.
DR STRING; 9606.ENSP00000417291; -.
DR iPTMnet; Q9BWE0; -.
DR PhosphoSitePlus; Q9BWE0; -.
DR BioMuta; REPIN1; -.
DR DMDM; 74761300; -.
DR EPD; Q9BWE0; -.
DR jPOST; Q9BWE0; -.
DR MassIVE; Q9BWE0; -.
DR MaxQB; Q9BWE0; -.
DR PaxDb; Q9BWE0; -.
DR PeptideAtlas; Q9BWE0; -.
DR PRIDE; Q9BWE0; -.
DR ProteomicsDB; 79270; -. [Q9BWE0-3]
DR ProteomicsDB; 8361; -.
DR Antibodypedia; 32865; 68 antibodies from 17 providers.
DR DNASU; 29803; -.
DR Ensembl; ENST00000397281.6; ENSP00000380451.2; ENSG00000214022.12. [Q9BWE0-3]
DR Ensembl; ENST00000425389.2; ENSP00000388287.2; ENSG00000214022.12. [Q9BWE0-3]
DR Ensembl; ENST00000444957.3; ENSP00000407714.1; ENSG00000214022.12. [Q9BWE0-3]
DR Ensembl; ENST00000489432.7; ENSP00000417291.2; ENSG00000214022.12. [Q9BWE0-4]
DR GeneID; 29803; -.
DR KEGG; hsa:29803; -.
DR MANE-Select; ENST00000489432.7; ENSP00000417291.2; NM_001099695.2; NP_001093165.1. [Q9BWE0-4]
DR UCSC; uc003whc.2; human. [Q9BWE0-3]
DR CTD; 29803; -.
DR DisGeNET; 29803; -.
DR GeneCards; REPIN1; -.
DR HGNC; HGNC:17922; REPIN1.
DR HPA; ENSG00000214022; Low tissue specificity.
DR MIM; 619039; gene.
DR neXtProt; NX_Q9BWE0; -.
DR OpenTargets; ENSG00000214022; -.
DR PharmGKB; PA134933473; -.
DR VEuPathDB; HostDB:ENSG00000214022; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162588; -.
DR HOGENOM; CLU_002678_36_0_1; -.
DR InParanoid; Q9BWE0; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9BWE0; -.
DR TreeFam; TF326846; -.
DR PathwayCommons; Q9BWE0; -.
DR SignaLink; Q9BWE0; -.
DR BioGRID-ORCS; 29803; 8 hits in 1098 CRISPR screens.
DR ChiTaRS; REPIN1; human.
DR GeneWiki; REPIN1; -.
DR GenomeRNAi; 29803; -.
DR Pharos; Q9BWE0; Tbio.
DR PRO; PR:Q9BWE0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BWE0; protein.
DR Bgee; ENSG00000214022; Expressed in right uterine tube and 199 other tissues.
DR ExpressionAtlas; Q9BWE0; baseline and differential.
DR Genevisible; Q9BWE0; HS.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR039705; REPIN1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24406:SF10; PTHR24406:SF10; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW DNA replication; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..567
FT /note="Replication initiator 1"
FT /id="PRO_0000274912"
FT ZN_FING 57..79
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 85..107
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 116..138
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 145..168
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 177..199
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 236..258
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..286
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 292..314
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 543..565
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 17..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1
FT /note="M -> MGIGVSLLLQFSLTPGGYRSVGRSRRCSRGSIPRNIPKRSWKKPHPQ
FT LCSLQAEEEPM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054069"
FT VARIANT 14
FT /note="L -> P (in dbSNP:rs3735165)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_030364"
FT VARIANT 49
FT /note="G -> R (in dbSNP:rs35090619)"
FT /id="VAR_052730"
FT VARIANT 88
FT /note="P -> S (in dbSNP:rs11553624)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030365"
FT VARIANT 92
FT /note="R -> H (in dbSNP:rs17173702)"
FT /id="VAR_030366"
FT VARIANT 97
FT /note="A -> V (in dbSNP:rs17173703)"
FT /id="VAR_030367"
FT CONFLICT 136
FT /note="R -> L (in Ref. 1; AAF26712)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="R -> Q (in Ref. 1; AAF26712)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="R -> Q (in Ref. 2; CAB53100)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="E -> A (in Ref. 2; CAB53100)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="A -> V (in Ref. 2; CAB53100)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="P -> S (in Ref. 2; CAB53100)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..397
FT /note="QH -> HD (in Ref. 1; AAF26712)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="R -> P (in Ref. 1; AAF26712)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="R -> P (in Ref. 1; AAF26712)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="A -> R (in Ref. 1; AAF26712)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="S -> R (in Ref. 2; CAB53100)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="P -> S (in Ref. 2; CAB53100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 63575 MW; 00D43EC28E176237 CRC64;
MLERRCRGPL AMGLAQPRLL SGPSQESPQT LGKESRGLRQ QGTSVAQSGA QAPGRAHRCA
HCRRHFPGWV ALWLHTRRCQ ARLPLPCPEC GRRFRHAPFL ALHRQVHAAA TPDLGFACHL
CGQSFRGWVA LVLHLRAHSA AKRPIACPKC ERRFWRRKQL RAHLRRCHPP APEARPFICG
NCGRSFAQWD QLVAHKRVHV AEALEEAAAK ALGPRPRGRP AVTAPRPGGD AVDRPFQCAC
CGKRFRHKPN LIAHRRVHTG ERPHQCPECG KRFTNKPYLT SHRRIHTGEK PYPCKECGRR
FRHKPNLLSH SKIHKRSEGS AQAAPGPGSP QLPAGPQESA AEPTPAVPLK PAQEPPPGAP
PEHPQDPIEA PPSLYSCDDC GRSFRLERFL RAHQRQHTGE RPFTCAECGK NFGKKTHLVA
HSRVHSGERP FACEECGRRF SQGSHLAAHR RDHAPDRPFV CPDCGKAFRH KPYLAAHRRI
HTGEKPYVCP DCGKAFSQKS NLVSHRRIHT GERPYACPDC DRSFSQKSNL ITHRKSHIRD
GAFCCAICGQ TFDDEERLLA HQKKHDV
