PRD15_HUMAN
ID PRD15_HUMAN Reviewed; 1507 AA.
AC P57071; E9PDJ6; E9PF37; E9PGL3; Q4W8S0; Q4W8S3; Q4W8S4; Q4W8S5; Q8N0X3;
AC Q8NEX0; Q9NQV3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 4.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=PR domain zinc finger protein 15 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=PR domain-containing protein 15 {ECO:0000305};
DE AltName: Full=Zinc finger protein 298;
GN Name=PRDM15 {ECO:0000312|HGNC:HGNC:13999};
GN Synonyms=C21orf83 {ECO:0000312|HGNC:HGNC:13999},
GN ZNF298 {ECO:0000312|HGNC:HGNC:13999};
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).
RX PubMed=12036298; DOI=10.1006/geno.2002.6782;
RA Gardiner K., Slavov D., Bechtel L., Davisson M.;
RT "Annotation of human chromosome 21 for relevance to Down syndrome: gene
RT structure and expression analysis.";
RL Genomics 79:833-843(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), VARIANT PRO-1481,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Thymus;
RX PubMed=15904895; DOI=10.1016/j.bbrc.2005.04.159;
RA Shibuya K., Kudoh J., Okui M., Shimizu N.;
RT "Identification of a novel zinc finger protein gene (ZNF298) in the GAP2 of
RT human chromosome 21q.";
RL Biochem. Biophys. Res. Commun. 332:557-568(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-1481.
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 [MRNA] OF 1-951 (ISOFORM 1).
RA Yang X.-H., Huang S.;
RT "A family of novel PR-domain (PRDM) genes as candidate tumor suppressors.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1136-1507 (ISOFORMS 1/2), AND VARIANT
RP PRO-1481.
RX PubMed=12036297; DOI=10.1006/geno.2002.6781;
RA Reymond A., Camargo A.A., Deutsch S., Stevenson B.J., Parmigiani R.B.,
RA Ucla C., Bettoni F., Rossier C., Lyle R., Guipponi M., de Souza S.,
RA Iseli C., Jongeneel C.V., Bucher P., Simpson A.J.G., Antonarakis S.E.;
RT "Nineteen additional unpredicted transcripts from human chromosome 21.";
RL Genomics 79:824-832(2002).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-883, 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 [8]
RP FUNCTION.
RX PubMed=28740264; DOI=10.1038/ng.3922;
RA Mzoughi S., Zhang J., Hequet D., Teo S.X., Fang H., Xing Q.R., Bezzi M.,
RA Seah M.K.Y., Ong S.L.M., Shin E.M., Wollmann H., Wong E.S.M.,
RA Al-Haddawi M., Stewart C.L., Tergaonkar V., Loh Y.H., Dunn N.R.,
RA Messerschmidt D.M., Guccione E.;
RT "PRDM15 safeguards naive pluripotency by transcriptionally regulating WNT
RT and MAPK-ERK signaling.";
RL Nat. Genet. 49:1354-1363(2017).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-883, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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: Sequence-specific DNA-binding transcriptional regulator.
CC Plays a role as a molecular node in a transcriptional network
CC regulating embryonic development and cell fate decision. Stimulates the
CC expression of upstream key transcriptional activators and repressors of
CC the Wnt/beta-catenin and MAPK/ERK pathways, respectively, that are
CC essential for naive pluripotency and self-renewal maintenance of
CC embryonic stem cells (ESCs). Specifically promotes SPRY1 and RSPO1
CC transcription activation through recognition and direct binding of a
CC specific DNA sequence in their promoter regions. Involved in early
CC embryo development (By similarity). Also plays a role in induced
CC pluripotent stem cells (iPSCs) reprogramming (PubMed:28740264).
CC {ECO:0000250|UniProtKB:E9Q8T2, ECO:0000269|PubMed:28740264}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15904895}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P57071-1; Sequence=Displayed;
CC Name=2; Synonyms=ZNF298b;
CC IsoId=P57071-2; Sequence=VSP_055110, VSP_055111, VSP_055113;
CC Name=3; Synonyms=ZNF298a;
CC IsoId=P57071-3; Sequence=VSP_055110, VSP_055111;
CC Name=4; Synonyms=ZNF298c;
CC IsoId=P57071-5; Sequence=VSP_055110, VSP_055111, VSP_055114,
CC VSP_055117;
CC Name=5; Synonyms=ZNF298d;
CC IsoId=P57071-6; Sequence=VSP_055110, VSP_055111, VSP_055112,
CC VSP_055115, VSP_055116;
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined.
CC {ECO:0000269|PubMed:15904895}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues.
CC {ECO:0000269|PubMed:15904895}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL60596.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM53515.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
CC Sequence=AAM53516.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
CC Sequence=BAA95527.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD99015.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD99016.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD99017.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD99018.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
CC Sequence=BAD99020.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
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DR EMBL; AY078498; AAL85487.2; -; mRNA.
DR EMBL; AB051812; BAD99015.1; ALT_INIT; mRNA.
DR EMBL; AB051813; BAD99016.1; ALT_INIT; mRNA.
DR EMBL; AB051814; BAD99017.1; ALT_INIT; mRNA.
DR EMBL; AB051814; BAD99018.1; ALT_SEQ; mRNA.
DR EMBL; AB051815; BAD99020.1; ALT_SEQ; mRNA.
DR EMBL; AB126081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001745; BAA95527.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP002955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09585.1; -; Genomic_DNA.
DR EMBL; AF276513; AAF78093.1; -; mRNA.
DR EMBL; AY063456; AAL60596.1; ALT_INIT; mRNA.
DR EMBL; AF426259; AAM53515.1; ALT_SEQ; mRNA.
DR EMBL; AF426260; AAM53516.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001035514.1; NM_001040424.2.
DR RefSeq; NP_001269863.1; NM_001282934.1.
DR RefSeq; NP_071398.3; NM_022115.4.
DR AlphaFoldDB; P57071; -.
DR BioGRID; 122024; 77.
DR IntAct; P57071; 10.
DR MINT; P57071; -.
DR STRING; 9606.ENSP00000269844; -.
DR iPTMnet; P57071; -.
DR PhosphoSitePlus; P57071; -.
DR BioMuta; PRDM15; -.
DR DMDM; 118572696; -.
DR EPD; P57071; -.
DR jPOST; P57071; -.
DR MassIVE; P57071; -.
DR MaxQB; P57071; -.
DR PaxDb; P57071; -.
DR PeptideAtlas; P57071; -.
DR PRIDE; P57071; -.
DR ProteomicsDB; 19680; -.
DR ProteomicsDB; 20018; -.
DR ProteomicsDB; 20339; -.
DR ProteomicsDB; 56980; -. [P57071-1]
DR Antibodypedia; 9262; 104 antibodies from 20 providers.
DR DNASU; 63977; -.
DR Ensembl; ENST00000269844.5; ENSP00000269844.4; ENSG00000141956.14.
DR Ensembl; ENST00000398548.6; ENSP00000381556.2; ENSG00000141956.14.
DR Ensembl; ENST00000422911.6; ENSP00000408592.2; ENSG00000141956.14.
DR Ensembl; ENST00000449395.6; ENSP00000396943.2; ENSG00000141956.14.
DR GeneID; 63977; -.
DR KEGG; hsa:63977; -.
DR UCSC; uc002yzo.4; human. [P57071-1]
DR CTD; 63977; -.
DR DisGeNET; 63977; -.
DR GeneCards; PRDM15; -.
DR HGNC; HGNC:13999; PRDM15.
DR HPA; ENSG00000141956; Low tissue specificity.
DR MIM; 617692; gene.
DR neXtProt; NX_P57071; -.
DR PharmGKB; PA33713; -.
DR VEuPathDB; HostDB:ENSG00000141956; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P57071; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P57071; -.
DR TreeFam; TF331419; -.
DR PathwayCommons; P57071; -.
DR SignaLink; P57071; -.
DR BioGRID-ORCS; 63977; 26 hits in 1102 CRISPR screens.
DR ChiTaRS; PRDM15; human.
DR GenomeRNAi; 63977; -.
DR Pharos; P57071; Tbio.
DR PRO; PR:P57071; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P57071; protein.
DR Bgee; ENSG00000141956; Expressed in sural nerve and 151 other tissues.
DR ExpressionAtlas; P57071; baseline and differential.
DR Genevisible; P57071; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd19199; PR-SET_PRDM15; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044409; PRDM15_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; DNA-binding;
KW Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..1507
FT /note="PR domain zinc finger protein 15"
FT /id="PRO_0000047772"
FT DOMAIN 415..525
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 563..585
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 738..760
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 765..788
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 826..848
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 853..875
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 902..924
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 929..951
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 992..1015
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1020..1042
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1056..1078
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1084..1106
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1112..1134
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1140..1162
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1168..1190
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1196..1219
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1225..1248
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1474..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 883
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 35..297
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055110"
FT VAR_SEQ 344..409
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055111"
FT VAR_SEQ 701..720
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055112"
FT VAR_SEQ 821
FT /note="T -> TGLIAHPGEGGPGGSRLRDLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055113"
FT VAR_SEQ 822..884
FT /note="DDKTFQCEMCFRFFSTNSNLSKHKKKHGDKKFACEVCSKMFYRKDVMLDHQR
FT RHLEGVRRVKR -> GLIAHPGEGGPGGSRLRDLPATSPSTRRSTATRSLPVRSAARCS
FT TARTSCWTTSAGTWKECGE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055114"
FT VAR_SEQ 822..864
FT /note="DDKTFQCEMCFRFFSTNSNLSKHKKKHGDKKFACEVCSKMFYR -> ATSPS
FT TRRSTATRSLPVRSAARCSTARTSCWTTSAGTWKECGE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055115"
FT VAR_SEQ 865..1507
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055116"
FT VAR_SEQ 885..1507
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15904895"
FT /id="VSP_055117"
FT VARIANT 1342
FT /note="V -> I (in dbSNP:rs3819158)"
FT /id="VAR_014992"
FT VARIANT 1376
FT /note="T -> S (in dbSNP:rs2236695)"
FT /id="VAR_014993"
FT VARIANT 1481
FT /note="S -> P (in dbSNP:rs3850706)"
FT /evidence="ECO:0000269|PubMed:12036297,
FT ECO:0000269|PubMed:15904895, ECO:0000269|Ref.4"
FT /id="VAR_014994"
FT CONFLICT 1147
FT /note="R -> G (in Ref. 6; AAL60596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="D -> I (in Ref. 6; AAL60596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1507 AA; 169269 MW; E980A7EDB97239D0 CRC64;
MPRRRPPASG AAQFPERIAT RSPDPIPLCT FQRQPRAAPV QPPCRLFFVT FAGCGHRWRS
ESKPGWISRS RSGIALRAAR PPGSSPPRPA APRPPPPGGV VAEAPGDVVI PRPRVQPMRV
ARGGPWTPNP AFREAESWSQ IGNQRVSEQL LETSLGNEVS DTEPLSPASA GLRRNPALPP
GPFAQNFSWG NQENLPPALG KIANGGGTGA GKAECGYETE SHLLEPHEIP LNVNTHKFSD
CEFPYEFCTV CFSPFKLLGM SGVEGVWNQH SRSASMHTFL NHSATGIREA GCRKDMPVSE
MAEDGSEEIM FIWCEDCSQY HDSECPELGP VVMVKDSFVL SRARSWPASG HVHTQAGQGM
RGYEDRDRAD PQQLPEAVPA GLVRRLSGQQ LPCRSTLTWG RLCHLVAQGR SSLPPNLEIR
RLEDGAEGVF AITQLVKRTQ FGPFESRRVA KWEKESAFPL KVFQKDGHPV CFDTSNEDDC
NWMMLVRPAA EAEHQNLTAY QHGSDVYFTT SRDIPPGTEL RVWYAAFYAK KMDKPMLKQA
GSGVHAAGTP ENSAPVESEP SQWACKVCSA TFLELQLLNE HLLGHLEQAK SLPPGSQSEA
AAPEKEQDTP RGEPPAVPES ENVATKEQKK KPRRGRKPKV SKAEQPLVIV EDKEPTEQVA
EIITEVPPDE PVSATPDERI MELVLGKLAT TTTDTSSVPK FTHHQNNTIT LKRSLILSSR
HGIRRKLIKQ LGEHKRVYQC NICSKIFQNS SNLSRHVRSH GDKLFKCEEC AKLFSRKESL
KQHVSYKHSR NEVDGEYRYR CGTCEKTFRI ESALEFHNCR TDDKTFQCEM CFRFFSTNSN
LSKHKKKHGD KKFACEVCSK MFYRKDVMLD HQRRHLEGVR RVKREDLEAG GENLVRYKKE
PSGCPVCGKV FSCRSNMNKH LLTHGDKKYT CEICGRKFFR VDVLRDHIHV HFKDIALMDD
HQREEFIGKI GISSEENDDN SDESADSEPH KYSCKRCQLT FGRGKEYLKH IMEVHKEKGY
GCSICNRRFA LKATYHAHMV IHRENLPDPN VQKYIHPCEI CGRIFNSIGN LERHKLIHTG
VKSHACEQCG KSFARKDMLK EHMRVHDNVR EYLCAECGKG MKTKHALRHH MKLHKGIKEY
ECKECHRRFA QKVNMLKHCK RHTGIKDFMC ELCGKTFSER NTMETHKLIH TVGKQWTCSV
CDKKYVTEYM LQKHVQLTHD KVEAQSCQLC GTKVSTRASM SRHMRRKHPE VLAVRIDDLD
HLPETTTIDA SSIGIVQPEL TLEQEDLAEG KHGKAAKRSH KRKQKPEEEA GAPVPEDATF
SEYSEKETEF TGSVGDETNS AVQSIQQVVV TLGDPNVTTP SSSVGLTNIT VTPITTAAAT
QFTNLQPVAV GHLTTPERQL QLDNSILTVT FDTVSGSAML HNRQNDVQIH PQPEASNPQS
VAHFINLTTL VNSITPLGSQ LSDQHPLTWR AVPQTDVLPP SQPQAPPQQA AQPQVQAEQQ
QQQMYSY
