DR4L2_HUMAN
ID DR4L2_HUMAN Reviewed; 232 AA.
AC Q6PKH6; H0YN69; Q3YLD4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dehydrogenase/reductase SDR family member 4-like 2 {ECO:0000303|PubMed:19027726};
DE EC=1.1.-.-;
DE AltName: Full=Short chain dehydrogenase/reductase family 25C member 3 {ECO:0000303|PubMed:19027726};
DE Short=Protein SDR25C3 {ECO:0000303|PubMed:19027726};
DE Flags: Precursor;
GN Name=DHRS4L2 {ECO:0000312|HGNC:HGNC:19731};
GN Synonyms=SDR25C3 {ECO:0000303|PubMed:19027726};
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 GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-19.
RC TISSUE=Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-232 (ISOFORM 2).
RX PubMed=16204458; DOI=10.1093/nar/gki870;
RA Hiller M., Huse K., Platzer M., Backofen R.;
RT "Non-EST based prediction of exon skipping and intron retention events
RT using Pfam information.";
RL Nucleic Acids Res. 33:5611-5621(2005).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
RN [5]
RP MISCELLANEOUS.
RX PubMed=27323117; DOI=10.4238/gmr.15027752;
RA Su Z., Liu G., Song X., Liang B., Chang X., Huang D.;
RT "CpG island evolution in the mammalian DHRS4 gene cluster and its role in
RT the regulation of gene transcription.";
RL Genet. Mol. Res. 15:0-0(2016).
CC -!- FUNCTION: Probable oxidoreductase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PKH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PKH6-2; Sequence=VSP_029697;
CC -!- MISCELLANEOUS: Three homologous proteins DHRS4, DHRS4L1, and DHRS4L2
CC are derived from gene duplication of DHRS4, and the gene cluster is
CC arranged in tandem in chromosome 14. {ECO:0000269|PubMed:27323117}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00663.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000663; AAH00663.2; ALT_INIT; mRNA.
DR EMBL; DQ088988; AAZ85982.1; -; mRNA.
DR CCDS; CCDS9606.2; -. [Q6PKH6-1]
DR AlphaFoldDB; Q6PKH6; -.
DR SMR; Q6PKH6; -.
DR IntAct; Q6PKH6; 6.
DR MINT; Q6PKH6; -.
DR STRING; 9606.ENSP00000334801; -.
DR DrugBank; DB04200; Matairesinol.
DR GlyGen; Q6PKH6; 1 site.
DR iPTMnet; Q6PKH6; -.
DR PhosphoSitePlus; Q6PKH6; -.
DR BioMuta; DHRS4L2; -.
DR DMDM; 74749268; -.
DR jPOST; Q6PKH6; -.
DR MassIVE; Q6PKH6; -.
DR MaxQB; Q6PKH6; -.
DR PaxDb; Q6PKH6; -.
DR PeptideAtlas; Q6PKH6; -.
DR PRIDE; Q6PKH6; -.
DR ProteomicsDB; 40471; -.
DR ProteomicsDB; 67244; -. [Q6PKH6-1]
DR ProteomicsDB; 67245; -. [Q6PKH6-2]
DR Antibodypedia; 22568; 122 antibodies from 14 providers.
DR Ensembl; ENST00000335125.11; ENSP00000334801.6; ENSG00000187630.18. [Q6PKH6-1]
DR Ensembl; ENST00000559411.5; ENSP00000453889.1; ENSG00000187630.18. [Q6PKH6-2]
DR GeneID; 317749; -.
DR MANE-Select; ENST00000335125.11; ENSP00000334801.6; NM_198083.4; NP_932349.2.
DR UCSC; uc001wli.5; human. [Q6PKH6-1]
DR CTD; 317749; -.
DR GeneCards; DHRS4L2; -.
DR HGNC; HGNC:19731; DHRS4L2.
DR HPA; ENSG00000187630; Tissue enhanced (liver).
DR MIM; 615196; gene.
DR neXtProt; NX_Q6PKH6; -.
DR OpenTargets; ENSG00000187630; -.
DR VEuPathDB; HostDB:ENSG00000187630; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000158919; -.
DR InParanoid; Q6PKH6; -.
DR PhylomeDB; Q6PKH6; -.
DR TreeFam; TF315405; -.
DR PathwayCommons; Q6PKH6; -.
DR SignaLink; Q6PKH6; -.
DR ChiTaRS; DHRS4L2; human.
DR Pharos; Q6PKH6; Tbio.
DR PRO; PR:Q6PKH6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q6PKH6; protein.
DR Bgee; ENSG00000187630; Expressed in right lobe of liver and 95 other tissues.
DR ExpressionAtlas; Q6PKH6; baseline and differential.
DR Genevisible; Q6PKH6; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0042574; P:retinal metabolic process; IBA:GO_Central.
DR InterPro; IPR029511; DHRS4-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43943:SF8; PTHR43943:SF8; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; NAD; NADP; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..232
FT /note="Dehydrogenase/reductase SDR family member 4-like 2"
FT /id="PRO_0000312103"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 36..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 222..232
FT /note="CSGWTRKKRKA -> WLGEPEDCAGIVSFLCSEDAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16204458"
FT /id="VSP_029697"
FT VARIANT 19
FT /note="M -> L (in dbSNP:rs2273947)"
FT /id="VAR_037395"
FT CONFLICT 2
FT /note="Q -> H (in Ref. 2; AAH00663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 24863 MW; A42B8CB0D791085A CRC64;
MQMARLLGLC AWARKSVRMA SSRMTRRDPL TNKVALVTAS TDGIGFAIAR RLAQDRAHVV
VSSRKQQNVD QAVATLQGEG LSVTGTVCHV GKAEDRERLV AMAVKLHGGI DILVSNAAVN
PFFGSLMDVT EEVWDKTLDI NVKAPALMTK AVVPEMEKRG GGSVVIVSSI AAFSPSPGFS
PYNVSKTALL GLNNTLAIEL APRNIRVNCL HLDLSRLASA GCSGWTRKKR KA
