DHR12_HUMAN
ID DHR12_HUMAN Reviewed; 317 AA.
AC A0PJE2; Q96GB2; Q9H8H1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dehydrogenase/reductase SDR family member 12 {ECO:0000303|PubMed:19027726};
DE EC=1.1.-.- {ECO:0000305};
DE AltName: Full=Short-chain dehydrogenase/reductase family 40C member 1 {ECO:0000303|PubMed:19027726};
DE Short=Protein SDR40C1 {ECO:0000303|PubMed:19027726};
GN Name=DHRS12 {ECO:0000312|HGNC:HGNC:25832};
GN Synonyms=SDR40C1 {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 MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 6-317 (ISOFORM 1).
RC TISSUE=Kidney, and Lung;
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 [5]
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).
CC -!- FUNCTION: Putative oxidoreductase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A0PJE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0PJE2-2; Sequence=VSP_029724, VSP_029726, VSP_029727;
CC Name=3;
CC IsoId=A0PJE2-3; Sequence=VSP_029724, VSP_029725;
CC Name=4;
CC IsoId=A0PJE2-4; Sequence=VSP_029724;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AK023701; BAB14646.1; -; mRNA.
DR EMBL; AL136525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08884.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08888.1; -; Genomic_DNA.
DR EMBL; BC009825; AAH09825.1; -; mRNA.
DR EMBL; BC026024; AAH26024.1; -; mRNA.
DR CCDS; CCDS31976.1; -. [A0PJE2-3]
DR CCDS; CCDS58292.1; -. [A0PJE2-1]
DR CCDS; CCDS9430.1; -. [A0PJE2-2]
DR RefSeq; NP_001026889.1; NM_001031719.2. [A0PJE2-3]
DR RefSeq; NP_001257353.1; NM_001270424.1. [A0PJE2-1]
DR RefSeq; NP_078981.1; NM_024705.2. [A0PJE2-2]
DR AlphaFoldDB; A0PJE2; -.
DR SMR; A0PJE2; -.
DR BioGRID; 122867; 16.
DR STRING; 9606.ENSP00000411565; -.
DR BioMuta; DHRS12; -.
DR MassIVE; A0PJE2; -.
DR PaxDb; A0PJE2; -.
DR PeptideAtlas; A0PJE2; -.
DR PRIDE; A0PJE2; -.
DR ProteomicsDB; 54; -. [A0PJE2-1]
DR Antibodypedia; 42326; 66 antibodies from 14 providers.
DR DNASU; 79758; -.
DR Ensembl; ENST00000218981.5; ENSP00000218981.1; ENSG00000102796.12. [A0PJE2-2]
DR Ensembl; ENST00000280056.6; ENSP00000280056.2; ENSG00000102796.12. [A0PJE2-3]
DR Ensembl; ENST00000444610.8; ENSP00000411565.3; ENSG00000102796.12. [A0PJE2-4]
DR GeneID; 79758; -.
DR KEGG; hsa:79758; -.
DR MANE-Select; ENST00000444610.8; ENSP00000411565.3; NM_001377533.1; NP_001364462.1. [A0PJE2-4]
DR UCSC; uc001vfq.5; human. [A0PJE2-1]
DR CTD; 79758; -.
DR DisGeNET; 79758; -.
DR GeneCards; DHRS12; -.
DR HGNC; HGNC:25832; DHRS12.
DR HPA; ENSG00000102796; Tissue enhanced (pancreas).
DR MIM; 616163; gene.
DR neXtProt; NX_A0PJE2; -.
DR OpenTargets; ENSG00000102796; -.
DR PharmGKB; PA147358124; -.
DR VEuPathDB; HostDB:ENSG00000102796; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000163782; -.
DR HOGENOM; CLU_010194_44_8_1; -.
DR InParanoid; A0PJE2; -.
DR OMA; FYRNTVW; -.
DR OrthoDB; 1076292at2759; -.
DR PhylomeDB; A0PJE2; -.
DR TreeFam; TF353029; -.
DR PathwayCommons; A0PJE2; -.
DR BioGRID-ORCS; 79758; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; DHRS12; human.
DR GenomeRNAi; 79758; -.
DR Pharos; A0PJE2; Tdark.
DR PRO; PR:A0PJE2; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; A0PJE2; protein.
DR Bgee; ENSG00000102796; Expressed in body of pancreas and 95 other tissues.
DR ExpressionAtlas; A0PJE2; baseline and differential.
DR Genevisible; A0PJE2; HS.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..317
FT /note="Dehydrogenase/reductase SDR family member 12"
FT /id="PRO_0000312175"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT VAR_SEQ 1..91
FT /note="MSLYRSVVWFAKGLREYTKSGYESACKDFVPHDLEVQIPGRVFLVTGGNSGI
FT GKATALEIAKRGGTVHLVCRDQAPAEDARGEIIRESGNQ -> MNLHVKTLSLMTWRSR
FT FLEESFWSLEETAALAKQLPLKSPSE (in isoform 2, isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029724"
FT VAR_SEQ 236..317
FT /note="GVRQAMPGFHARFGDRLRSEAQGADTMLWLALSSAAAAQPSGRFFQDRKPVS
FT THLPLATASSSPAEEEKLIEILEQLAQTFK -> DRNEQELRKVVGEAQTASPLPRFLE
FT IMMHEGKCQPQGHSSNDLEACWSSGGGEQNSLPDWPHQLHDLRQLTWALCSSFLLYKQG
FT N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029725"
FT VAR_SEQ 282..296
FT /note="DRKPVSTHLPLATAS -> GDFLPGCEGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029726"
FT VAR_SEQ 297..317
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029727"
SQ SEQUENCE 317 AA; 35146 MW; C5BCF344FB4625D4 CRC64;
MSLYRSVVWF AKGLREYTKS GYESACKDFV PHDLEVQIPG RVFLVTGGNS GIGKATALEI
AKRGGTVHLV CRDQAPAEDA RGEIIRESGN QNIFLHIVDL SDPKQIWKFV ENFKQEHKLH
VLINNAGCMV NKRELTEDGL EKNFAANTLG VYILTTGLIP VLEKEHDPRV ITVSSGGMLV
QKLNTNDLQS ERTPFDGTMV YAQNKRQQVV LTERWAQGHP AIHFSSMHPG WADTPGVRQA
MPGFHARFGD RLRSEAQGAD TMLWLALSSA AAAQPSGRFF QDRKPVSTHL PLATASSSPA
EEEKLIEILE QLAQTFK
