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   24-JAN-2024, entry version 205.
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; 81.
DR   IntAct; P57071; 10.
DR   MINT; P57071; -.
DR   STRING; 9606.ENSP00000269844; -.
DR   GlyGen; P57071; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000269844; -.
DR   PeptideAtlas; P57071; -.
DR   ProteomicsDB; 19680; -.
DR   ProteomicsDB; 20018; -.
DR   ProteomicsDB; 20339; -.
DR   ProteomicsDB; 56980; -. [P57071-1]
DR   Pumba; P57071; -.
DR   Antibodypedia; 9262; 113 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   MANE-Select; ENST00000398548.6; ENSP00000381556.2; NM_001040424.3; NP_001035514.2.
DR   UCSC; uc002yzo.4; human. [P57071-1]
DR   AGR; HGNC:13999; -.
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; 5400229at2759; -.
DR   PhylomeDB; P57071; -.
DR   TreeFam; TF331419; -.
DR   PathwayCommons; P57071; -.
DR   SignaLink; P57071; -.
DR   BioGRID-ORCS; 63977; 28 hits in 1180 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 152 other cell types or 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; 3.30.160.60; Classic Zinc Finger; 11.
DR   Gene3D; 2.170.270.10; SET domain; 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   PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR16515:SF34; PR DOMAIN ZINC FINGER PROTEIN 15; 1.
DR   Pfam; PF21549; PRDM2_PR; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00355; ZnF_C2H2; 17.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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
//