ZNF48_HUMAN
ID ZNF48_HUMAN Reviewed; 618 AA.
AC Q96MX3; Q15920; Q4G0R3; Q69YP3; Q96IL9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc finger protein 48;
DE AltName: Full=Zinc finger protein 553;
GN Name=ZNF48; Synonyms=ZNF553;
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], AND VARIANT VAL-65.
RC TISSUE=Hippocampus;
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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-65.
RC TISSUE=Brain, and 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-182.
RC TISSUE=Placenta;
RX PubMed=1505991; DOI=10.1016/0888-7543(92)90013-i;
RA Lichter P., Bray P., Ried T., Dawid I.B., Ward D.C.;
RT "Clustering of C2-H2 zinc finger motif sequences within telomeric and
RT fragile site regions of human chromosomes.";
RL Genomics 13:999-1007(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-618, AND VARIANT VAL-65.
RC TISSUE=Melanoma;
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 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-610, 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-610, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-610, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-179; LYS-269; LYS-329;
RP LYS-477 AND LYS-610, 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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q96MX3; Q9NRW3: APOBEC3C; NbExp=3; IntAct=EBI-12006434, EBI-1044593;
CC Q96MX3; Q13895: BYSL; NbExp=3; IntAct=EBI-12006434, EBI-358049;
CC Q96MX3; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-12006434, EBI-747776;
CC Q96MX3; P60228: EIF3E; NbExp=3; IntAct=EBI-12006434, EBI-347740;
CC Q96MX3; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-12006434, EBI-744935;
CC Q96MX3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12006434, EBI-618309;
CC Q96MX3; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12006434, EBI-5916454;
CC Q96MX3; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-12006434, EBI-10961706;
CC Q96MX3; Q15014: MORF4L2; NbExp=3; IntAct=EBI-12006434, EBI-399257;
CC Q96MX3; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-12006434, EBI-11522433;
CC Q96MX3; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-12006434, EBI-1051317;
CC Q96MX3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-12006434, EBI-1567797;
CC Q96MX3; Q15427: SF3B4; NbExp=3; IntAct=EBI-12006434, EBI-348469;
CC Q96MX3; O75410-7: TACC1; NbExp=3; IntAct=EBI-12006434, EBI-12007872;
CC Q96MX3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-12006434, EBI-11741437;
CC Q96MX3; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-12006434, EBI-725997;
CC Q96MX3; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-12006434, EBI-12006434;
CC Q96MX3; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-12006434, EBI-10251462;
CC Q96MX3; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-12006434, EBI-10240849;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61316.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK056313; BAB71146.1; -; mRNA.
DR EMBL; AC116348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007393; AAH07393.2; -; mRNA.
DR EMBL; BC041388; AAH41388.1; -; mRNA.
DR EMBL; M88358; AAA61316.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL832433; CAH10657.1; -; mRNA.
DR CCDS; CCDS10679.1; -.
DR PIR; B43284; B43284.
DR RefSeq; NP_001201835.1; NM_001214906.1.
DR RefSeq; NP_001201838.1; NM_001214909.1.
DR RefSeq; NP_689865.2; NM_152652.2.
DR AlphaFoldDB; Q96MX3; -.
DR SMR; Q96MX3; -.
DR BioGRID; 128257; 153.
DR IntAct; Q96MX3; 33.
DR STRING; 9606.ENSP00000480262; -.
DR iPTMnet; Q96MX3; -.
DR PhosphoSitePlus; Q96MX3; -.
DR BioMuta; ZNF48; -.
DR DMDM; 296453060; -.
DR EPD; Q96MX3; -.
DR jPOST; Q96MX3; -.
DR MassIVE; Q96MX3; -.
DR MaxQB; Q96MX3; -.
DR PaxDb; Q96MX3; -.
DR PeptideAtlas; Q96MX3; -.
DR PRIDE; Q96MX3; -.
DR ProteomicsDB; 77428; -.
DR TopDownProteomics; Q96MX3; -.
DR Antibodypedia; 13692; 32 antibodies from 15 providers.
DR DNASU; 197407; -.
DR Ensembl; ENST00000320159.2; ENSP00000324056.2; ENSG00000180035.13.
DR Ensembl; ENST00000613509.2; ENSP00000480262.1; ENSG00000180035.13.
DR GeneID; 197407; -.
DR KEGG; hsa:197407; -.
DR MANE-Select; ENST00000613509.2; ENSP00000480262.1; NM_001214909.2; NP_001201838.1.
DR UCSC; uc002dya.2; human.
DR CTD; 197407; -.
DR GeneCards; ZNF48; -.
DR HGNC; HGNC:13114; ZNF48.
DR HPA; ENSG00000180035; Low tissue specificity.
DR neXtProt; NX_Q96MX3; -.
DR OpenTargets; ENSG00000180035; -.
DR PharmGKB; PA37689; -.
DR VEuPathDB; HostDB:ENSG00000180035; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162332; -.
DR InParanoid; Q96MX3; -.
DR OMA; QTWDDLW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96MX3; -.
DR TreeFam; TF338489; -.
DR PathwayCommons; Q96MX3; -.
DR SignaLink; Q96MX3; -.
DR BioGRID-ORCS; 197407; 21 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF48; human.
DR GenomeRNAi; 197407; -.
DR Pharos; Q96MX3; Tdark.
DR PRO; PR:Q96MX3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96MX3; protein.
DR Bgee; ENSG00000180035; Expressed in cortical plate and 163 other tissues.
DR ExpressionAtlas; Q96MX3; baseline and differential.
DR Genevisible; Q96MX3; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..618
FT /note="Zinc finger protein 48"
FT /id="PRO_0000234586"
FT ZN_FING 112..134
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 140..162
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..214
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 220..242
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 275..297
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 303..325
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 331..353
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 359..381
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 451..473
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 479..501
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 543..565
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 571..593
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q3US17"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 610
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 21
FT /note="Q -> R (in dbSNP:rs7200143)"
FT /id="VAR_059894"
FT VARIANT 65
FT /note="A -> V (in dbSNP:rs12921440)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_052758"
FT VARIANT 224
FT /note="I -> V (in dbSNP:rs34843513)"
FT /id="VAR_052759"
FT CONFLICT 12
FT /note="L -> I (in Ref. 2; AAH41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Y -> C (in Ref. 2; AAH41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="Q -> L (in Ref. 1; BAB71146)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="S -> P (in Ref. 2; AAH41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="R -> H (in Ref. 2; AAH41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="H -> R (in Ref. 2; AAH41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="R -> H (in Ref. 2; AAH41388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 67820 MW; B31CB196816B2D93 CRC64;
MERAVEPWGP DLHRPEEREP QRGARTGLGS ENVISQPNEF EHTPQEDDLG FKEEDLAPDH
EVGNASLKPE GIQNWDDLWV QREGLGKPQP RDRGPRLLGE PRWGQASSDR AAVCGECGKS
FRQMSDLVKH QRTHTGEKPY KCGVCGKGFG DSSARIKHQR THSGEKPYRA RPPAQGPPKI
PRSRIPAGER PTICGECGKS FRQSSDLVKH QRTHTGEKPY KCGICGKGFG DSSARIKHQR
THRGEQPPRP VVPRRQPSRA ATAATQGPKA QDKPYICTDC GKRFVLSCSL LSHQRSHLGP
KPFGCDVCGK EFARGSDLVK HLRVHTGEKP YLCPECGKGF ADSSARVKHL RTHSGERPHA
CPECDRTFSL SSTLLRHRLT HMEPQDFSFP GYPLPALIPS PPPPPLGTSP PLTPRSPSHS
GEPFGLPGLE PEPGGPQAGE PPPPLAGDKP HKCPECGKGF RRSSDLVKHH RVHTGEKPYL
CPECGKGFAD SSARVKHLRT HRGERARPPP PSTLLRPHNP PGPVPMAPRP RVRAQPSGPS
QPHVCGFCGK EFPRSSDLVK HRRTHTGEKP YKCAECGKGF GDSSARIKHQ RGHLVLTPFG
IGDGRARPLK QEAATGLE
