ZNF91_HUMAN
ID ZNF91_HUMAN Reviewed; 1191 AA.
AC Q05481; A8K5E1; B7Z6G6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Zinc finger protein 91;
DE AltName: Full=Zinc finger protein HPF7;
DE AltName: Full=Zinc finger protein HTF10;
GN Name=ZNF91;
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), AND VARIANTS ALA-336 AND THR-386.
RX PubMed=8467795; DOI=10.1002/j.1460-2075.1993.tb05781.x;
RA Bellefroid E.J., Marine J.-C., Ried T., Lecocq P.J., Riviere M.,
RA Amemiya C.T., Poncelet D.A., Coulie P.G., de Jong P.J., Szpirer C.,
RA Ward D.C., Martial J.A.;
RT "Clustered organization of homologous KRAB zinc-finger genes with enhanced
RT expression in human T lymphoid cells.";
RL EMBO J. 12:1363-1374(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-386.
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-204 (ISOFORM 1).
RX PubMed=2023909; DOI=10.1073/pnas.88.9.3608;
RA Bellefroid E.J., Poncelet D.A., Lecocq P.J., Revelant O., Martial J.A.;
RT "The evolutionarily conserved Kruppel-associated box domain defines a
RT subfamily of eukaryotic multifingered proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3608-3612(1991).
RN [5]
RP IDENTIFICATION.
RX PubMed=7479878; DOI=10.1073/pnas.92.23.10757;
RA Bellefroid E.J., Marine J.C., Matera A.G., Bourguignon C., Desai T.,
RA Healy K.C., Bray-Ward P., Martial J.A., Ihle J.N., Ward D.C.;
RT "Emergence of the ZNF91 Kruppel-associated box-containing zinc finger gene
RT family in the last common ancestor of anthropoidea.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10757-10761(1995).
RN [6]
RP FUNCTION.
RX PubMed=11470777; DOI=10.1093/intimm/13.8.1075;
RA Nishimura T., Narita T., Miyazaki E., Ito T., Nishimoto N., Yoshizaki K.,
RA Martial J.A., Bellfroid E.J., Vissing H., Taniyama T.;
RT "Characterization of the human Fc gamma RIIB gene promoter: human zinc-
RT finger proteins (ZNF140 and ZNF91) that bind to different regions function
RT as transcription repressors.";
RL Int. Immunol. 13:1075-1084(2001).
RN [7]
RP IDENTIFICATION.
RX PubMed=16606703; DOI=10.1101/gr.4843906;
RA Hamilton A.T., Huntley S., Tran-Gyamfi M., Baggott D.M., Gordon L.,
RA Stubbs L.;
RT "Evolutionary expansion and divergence in the ZNF91 subfamily of primate-
RT specific zinc finger genes.";
RL Genome Res. 16:584-594(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23665872; DOI=10.1007/s00018-013-1359-4;
RA Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M.,
RA Huang Z.;
RT "Novel activity of KRAB domain that functions to reinforce nuclear
RT localization of KRAB-containing zinc finger proteins by interacting with
RT KAP1.";
RL Cell. Mol. Life Sci. 70:3947-3958(2013).
RN [9]
RP FUNCTION.
RX PubMed=25274305; DOI=10.1038/nature13760;
RA Jacobs F.M., Greenberg D., Nguyen N., Haeussler M., Ewing A.D., Katzman S.,
RA Paten B., Salama S.R., Haussler D.;
RT "An evolutionary arms race between KRAB zinc-finger genes ZNF91/93 and
RT SVA/L1 retrotransposons.";
RL Nature 516:242-245(2014).
CC -!- FUNCTION: Transcription factor specifically required to repress SINE-
CC VNTR-Alu (SVA) retrotransposons: recognizes and binds SVA sequences and
CC represses their expression by recruiting a repressive complex
CC containing TRIM28/KAP1 (PubMed:25274305). May also bind the promoter of
CC the FCGR2B gene, leading to repress its expression; however, additional
CC evidence is required to confirm this result in vivo (PubMed:11470777).
CC {ECO:0000269|PubMed:25274305, ECO:0000305|PubMed:11470777}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23665872}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q05481-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05481-2; Sequence=VSP_040288;
CC -!- MISCELLANEOUS: ZNF91 is only present in primates and emerged in the
CC last common ancestor of humans and Old-World monkeys. It underwent
CC structural changes between 8-12 Million years ago, probably to improve
CC the protein's ability to bind and repress SINE-VNTR-Alu (SVA)
CC retrotransposons elements (PubMed:25274305).
CC {ECO:0000269|PubMed:25274305, ECO:0000305|PubMed:16606703,
CC ECO:0000305|PubMed:7479878}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58672.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L11672; AAA59469.1; -; mRNA.
DR EMBL; AK300294; BAH13252.1; -; mRNA.
DR EMBL; AK291256; BAF83945.1; -; mRNA.
DR EMBL; AC010300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M61871; AAA58672.1; ALT_FRAME; mRNA.
DR CCDS; CCDS42541.1; -. [Q05481-1]
DR CCDS; CCDS74322.1; -. [Q05481-2]
DR PIR; F39384; F39384.
DR PIR; PQ0636; PQ0636.
DR PIR; S35305; S35305.
DR RefSeq; NP_001287880.1; NM_001300951.1. [Q05481-2]
DR RefSeq; NP_003421.2; NM_003430.3. [Q05481-1]
DR AlphaFoldDB; Q05481; -.
DR SMR; Q05481; -.
DR BioGRID; 113460; 11.
DR IntAct; Q05481; 7.
DR STRING; 9606.ENSP00000300619; -.
DR GlyGen; Q05481; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q05481; -.
DR PhosphoSitePlus; Q05481; -.
DR BioMuta; ZNF91; -.
DR DMDM; 313104067; -.
DR EPD; Q05481; -.
DR jPOST; Q05481; -.
DR MassIVE; Q05481; -.
DR MaxQB; Q05481; -.
DR PaxDb; Q05481; -.
DR PeptideAtlas; Q05481; -.
DR PRIDE; Q05481; -.
DR ProteomicsDB; 58328; -. [Q05481-1]
DR ProteomicsDB; 58329; -. [Q05481-2]
DR Antibodypedia; 28756; 110 antibodies from 12 providers.
DR DNASU; 7644; -.
DR Ensembl; ENST00000300619.12; ENSP00000300619.6; ENSG00000167232.14. [Q05481-1]
DR Ensembl; ENST00000397082.2; ENSP00000380272.2; ENSG00000167232.14. [Q05481-2]
DR GeneID; 7644; -.
DR KEGG; hsa:7644; -.
DR MANE-Select; ENST00000300619.12; ENSP00000300619.6; NM_003430.4; NP_003421.2.
DR UCSC; uc002nre.4; human. [Q05481-1]
DR CTD; 7644; -.
DR DisGeNET; 7644; -.
DR GeneCards; ZNF91; -.
DR HGNC; HGNC:13166; ZNF91.
DR HPA; ENSG00000167232; Tissue enhanced (brain).
DR MIM; 603971; gene.
DR neXtProt; NX_Q05481; -.
DR OpenTargets; ENSG00000167232; -.
DR PharmGKB; PA37739; -.
DR VEuPathDB; HostDB:ENSG00000167232; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161942; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q05481; -.
DR OMA; WHKRLHT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q05481; -.
DR TreeFam; TF343410; -.
DR PathwayCommons; Q05481; -.
DR SignaLink; Q05481; -.
DR SIGNOR; Q05481; -.
DR BioGRID-ORCS; 7644; 46 hits in 1028 CRISPR screens.
DR ChiTaRS; ZNF91; human.
DR GenomeRNAi; 7644; -.
DR Pharos; Q05481; Tbio.
DR PRO; PR:Q05481; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q05481; protein.
DR Bgee; ENSG00000167232; Expressed in type B pancreatic cell and 208 other tissues.
DR ExpressionAtlas; Q05481; baseline and differential.
DR Genevisible; Q05481; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0070895; P:negative regulation of transposon integration; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 29.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 34.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 19.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 31.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 35.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1191
FT /note="Zinc finger protein 91"
FT /id="PRO_0000047400"
FT DOMAIN 13..84
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 154..176
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 179..200
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 208..232
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 238..260
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 266..288
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..344
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 406..428
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..456
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 462..484
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 490..512
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..540
FT /note="C2H2-type 14; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 574..596
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 602..624
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 630..652
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 658..680
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 686..708
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 714..736
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 742..764
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 770..792
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 798..820
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 826..848
FT /note="C2H2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 854..876
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 885..904
FT /note="C2H2-type 27; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 910..932
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 938..960
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 966..988
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 994..1016
FT /note="C2H2-type 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1022..1044
FT /note="C2H2-type 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1050..1072
FT /note="C2H2-type 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1078..1100
FT /note="C2H2-type 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1106..1128
FT /note="C2H2-type 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1134..1156
FT /note="C2H2-type 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 55..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040288"
FT VARIANT 112
FT /note="Y -> H (in dbSNP:rs296091)"
FT /id="VAR_057393"
FT VARIANT 336
FT /note="T -> A (in dbSNP:rs449447)"
FT /evidence="ECO:0000269|PubMed:8467795"
FT /id="VAR_060417"
FT VARIANT 386
FT /note="A -> T (in dbSNP:rs403356)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8467795"
FT /id="VAR_060418"
FT VARIANT 455
FT /note="F -> I (in dbSNP:rs440638)"
FT /id="VAR_059897"
FT VARIANT 521
FT /note="E -> K (in dbSNP:rs12976753)"
FT /id="VAR_060419"
FT VARIANT 896
FT /note="T -> A (in dbSNP:rs296093)"
FT /id="VAR_057394"
FT VARIANT 1011
FT /note="R -> I (in dbSNP:rs1821844)"
FT /id="VAR_060420"
FT VARIANT 1033
FT /note="R -> Q (in dbSNP:rs1821846)"
FT /id="VAR_060421"
FT VARIANT 1164
FT /note="L -> P (in dbSNP:rs428549)"
FT /id="VAR_059898"
FT VARIANT 1164
FT /note="L -> V (in dbSNP:rs385750)"
FT /id="VAR_059899"
FT CONFLICT 142
FT /note="L -> F (in Ref. 2; BAH13252)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> H (in Ref. 1; AAA59469)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="A -> G (in Ref. 1; AAA59469)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="E -> V (in Ref. 2; BAF83945)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="C -> R (in Ref. 2; BAF83945)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="H -> R (in Ref. 2; BAH13252)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="E -> G (in Ref. 2; BAH13252)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="T -> P (in Ref. 1; AAA59469)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="G -> C (in Ref. 1; AAA59469)"
FT /evidence="ECO:0000305"
FT CONFLICT 1164
FT /note="L -> A (in Ref. 2; BAF83945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1191 AA; 137217 MW; B8F5F0327A79EE3B CRC64;
MPGTPGSLEM GLLTFRDVAI EFSPEEWQCL DTAQQNLYRN VMLENYRNLA FLGIALSKPD
LITYLEQGKE PWNMKQHEMV DEPTGICPHF PQDFWPEQSM EDSFQKVLLR KYEKCGHENL
QLRKGCKSVD ECKVHKEGYN KLNQCLTTAQ SKVFQCGKYL KVFYKFLNSN RHTIRHTGKK
CFKCKKCVKS FCIRLHKTQH KCVYITEKSC KCKECEKTFH WSSTLTNHKE IHTEDKPYKC
EECGKAFKQL STLTTHKIIC AKEKIYKCEE CGKAFLWSST LTRHKRIHTG EKPYKCEECG
KAFSHSSTLA KHKRIHTGEK PYKCEECGKA FSRSSTLAKH KRIHTGEKPY KCKECGKAFS
NSSTLANHKI THTEEKPYKC KECDKAFKRL STLTKHKIIH AGEKLYKCEE CGKAFNRSSN
LTIHKFIHTG EKPYKCEECG KAFNWSSSLT KHKRFHTREK PFKCKECGKA FIWSSTLTRH
KRIHTGEKPY KCEECGKAFR QSSTLTKHKI IHTGEKPYKF EECGKAFRQS LTLNKHKIIH
SREKPYKCKE CGKAFKQFST LTTHKIIHAG KKLYKCEECG KAFNHSSSLS THKIIHTGEK
SYKCEECGKA FLWSSTLRRH KRIHTGEKPY KCEECGKAFS HSSALAKHKR IHTGEKPYKC
KECGKAFSNS STLANHKITH TEEKPYKCKE CDKTFKRLST LTKHKIIHAG EKLYKCEECG
KAFNRSSNLT IHKFIHTGEK PYKCEECGKA FNWSSSLTKH KRIHTREKPF KCKECGKAFI
WSSTLTRHKR IHTGEKPYKC EECGKAFSRS STLTKHKTIH TGEKPYKCKE CGKAFKHSSA
LAKHKIIHAG EKLYKCEECG KAFNQSSNLT THKIIHTKEK PSKSEECDKA FIWSSTLTEH
KRIHTREKTY KCEECGKAFS QPSHLTTHKR MHTGEKPYKC EECGKAFSQS STLTTHKIIH
TGEKPYKCEE CGKAFRKSST LTEHKIIHTG EKPYKCEECG KAFSQSSTLT RHTRMHTGEK
PYKCEECGKA FNRSSKLTTH KIIHTGEKPY KCEECGKAFI SSSTLNGHKR IHTREKPYKC
EECGKAFSQS STLTRHKRLH TGEKPYKCGE CGKAFKESSA LTKHKIIHTG EKPYKCEKCG
KAFNQSSILT NHKKIHTITP VIPLLWEAEA GGSRGQEMET ILANTVKPLL Y
