ID DHRS1_HUMAN Reviewed; 313 AA.
AC Q96LJ7; D3DS71; Q8NDG3; Q96B59; Q96CQ5;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Dehydrogenase/reductase SDR family member 1 {ECO:0000303|PubMed:12153138};
DE EC=1.1.1.- {ECO:0000269|PubMed:30031147};
DE AltName: Full=Short chain dehydrogenase/reductase family 19C member 1 {ECO:0000303|PubMed:19027726};
DE Short=Protein SDR19C1 {ECO:0000303|PubMed:19027726};
GN Name=DHRS1 {ECO:0000312|HGNC:HGNC:16445}; Synonyms=SDR19C1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12153138; DOI=10.1023/a:1015722001960;
RA Wu Q., Xu M., Cheng C., Zhou Z., Huang Y., Zhao W., Zeng L., Xu J., Fu X.,
RA Ying K., Xie Y., Mao Y.;
RT "Molecular cloning and characterization of a novel dehydrogenase/reductase
RT (SDR family) member 1 gene from human fetal brain.";
RL Mol. Biol. Rep. 28:193-198(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, 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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=30031147; DOI=10.1016/j.jsbmb.2018.07.013;
RA Zemanova L., Navratilova H., Andrys R., Sperkova K., Andrejs J.,
RA Kozakova K., Meier M., Moeller G., Novotna E., Safr M., Adamski J.,
RA Wsol V.;
RT "Initial characterization of human DHRS1 (SDR19C1), a member of the short-
RT chain dehydrogenase/reductase superfamily.";
RL J. Steroid Biochem. Mol. Biol. 185:80-89(2019).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-262.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human SDR family member 1.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction
CC of steroids (estrone, androstene-3,17-dione and cortisone) as well as
CC prostaglandin E1, isatin and xenobiotics in vitro (PubMed:30031147).
CC May have a role in steroid and/or xenobiotic metabolism
CC (PubMed:30031147). {ECO:0000269|PubMed:30031147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC Xref=Rhea:RHEA:16705, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000305|PubMed:30031147};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16707;
CC Evidence={ECO:0000305|PubMed:30031147};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000305|PubMed:30031147};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14983;
CC Evidence={ECO:0000305|PubMed:30031147};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + prostaglandin E1 = NADP(+) + prostaglandin F1;
CC Xref=Rhea:RHEA:68612, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:178049;
CC Evidence={ECO:0000305|PubMed:30031147};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68613;
CC Evidence={ECO:0000305|PubMed:30031147};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + isatin + NADPH = 3-hydroxyindolin-2-one + NADP(+);
CC Xref=Rhea:RHEA:68608, ChEBI:CHEBI:15378, ChEBI:CHEBI:27539,
CC ChEBI:CHEBI:28536, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:30031147};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68609;
CC Evidence={ECO:0000305|PubMed:30031147};
CC -!- INTERACTION:
CC Q96LJ7; Q12982: BNIP2; NbExp=3; IntAct=EBI-746300, EBI-752094;
CC Q96LJ7; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-746300, EBI-517508;
CC Q96LJ7; O76011: KRT34; NbExp=3; IntAct=EBI-746300, EBI-1047093;
CC Q96LJ7; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-746300, EBI-11959885;
CC Q96LJ7; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-746300, EBI-11749135;
CC Q96LJ7; P60410: KRTAP10-8; NbExp=8; IntAct=EBI-746300, EBI-10171774;
CC Q96LJ7; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-746300, EBI-10172052;
CC Q96LJ7; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-746300, EBI-1052037;
CC Q96LJ7; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-746300, EBI-10210845;
CC Q96LJ7; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-746300, EBI-10176379;
CC Q96LJ7; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-746300, EBI-11953334;
CC Q96LJ7; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-746300, EBI-751260;
CC Q96LJ7; Q9BYQ7: KRTAP4-1; NbExp=3; IntAct=EBI-746300, EBI-34579671;
CC Q96LJ7; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-746300, EBI-10302392;
CC Q96LJ7; Q6L8H4: KRTAP5-1; NbExp=3; IntAct=EBI-746300, EBI-12074540;
CC Q96LJ7; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-746300, EBI-11958178;
CC Q96LJ7; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-746300, EBI-3958099;
CC Q96LJ7; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-746300, EBI-11962084;
CC Q96LJ7; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-746300, EBI-11958364;
CC Q96LJ7; P13473-2: LAMP2; NbExp=3; IntAct=EBI-746300, EBI-21591415;
CC Q96LJ7; O14633: LCE2B; NbExp=3; IntAct=EBI-746300, EBI-11478468;
CC Q96LJ7; Q969G2: LHX4; NbExp=3; IntAct=EBI-746300, EBI-2865388;
CC Q96LJ7; Q99750: MDFI; NbExp=4; IntAct=EBI-746300, EBI-724076;
CC Q96LJ7; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-746300, EBI-11522433;
CC Q96LJ7; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-746300, EBI-945833;
CC Q96LJ7; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-746300, EBI-22310682;
CC Q96LJ7; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-746300, EBI-5280197;
CC Q96LJ7; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-746300, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:30031147}. Note=May be attached to the ER membrane
CC by its C-terminus segment. {ECO:0000269|PubMed:30031147}.
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, adrenal glands, and at
CC low levels in skeletal muscle, kidney, pancreas and brain.
CC {ECO:0000269|PubMed:12153138, ECO:0000269|PubMed:30031147}.
CC -!- DOMAIN: May be attached to the ER membrane by its C-terminus segment.
CC {ECO:0000269|PubMed:30031147}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF418205; AAN32660.1; -; mRNA.
DR EMBL; BX247980; CAD62314.1; -; mRNA.
DR EMBL; AK058159; BAB71694.1; -; mRNA.
DR EMBL; AL833917; CAD38773.1; -; mRNA.
DR EMBL; CH471078; EAW66036.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66037.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66040.1; -; Genomic_DNA.
DR EMBL; BC014057; AAH14057.1; -; mRNA.
DR EMBL; BC015943; AAH15943.1; -; mRNA.
DR CCDS; CCDS9623.1; -.
DR RefSeq; NP_001129522.1; NM_001136050.2.
DR RefSeq; NP_612461.1; NM_138452.2.
DR PDB; 2QQ5; X-ray; 1.80 A; A=3-262.
DR PDBsum; 2QQ5; -.
DR AlphaFoldDB; Q96LJ7; -.
DR SMR; Q96LJ7; -.
DR BioGRID; 125457; 53.
DR IntAct; Q96LJ7; 30.
DR MINT; Q96LJ7; -.
DR STRING; 9606.ENSP00000380027; -.
DR iPTMnet; Q96LJ7; -.
DR PhosphoSitePlus; Q96LJ7; -.
DR SwissPalm; Q96LJ7; -.
DR BioMuta; DHRS1; -.
DR DMDM; 37999854; -.
DR EPD; Q96LJ7; -.
DR jPOST; Q96LJ7; -.
DR MassIVE; Q96LJ7; -.
DR MaxQB; Q96LJ7; -.
DR PaxDb; 9606-ENSP00000288111; -.
DR PeptideAtlas; Q96LJ7; -.
DR ProteomicsDB; 77214; -.
DR Pumba; Q96LJ7; -.
DR Antibodypedia; 23; 185 antibodies from 28 providers.
DR DNASU; 115817; -.
DR Ensembl; ENST00000288111.12; ENSP00000288111.7; ENSG00000157379.14.
DR Ensembl; ENST00000396813.5; ENSP00000380027.1; ENSG00000157379.14.
DR Ensembl; ENST00000644514.2; ENSP00000496132.1; ENSG00000284868.2.
DR Ensembl; ENST00000647514.1; ENSP00000493735.1; ENSG00000284868.2.
DR GeneID; 115817; -.
DR KEGG; hsa:115817; -.
DR MANE-Select; ENST00000288111.12; ENSP00000288111.7; NM_001136050.3; NP_001129522.1.
DR UCSC; uc001woj.3; human.
DR AGR; HGNC:16445; -.
DR CTD; 115817; -.
DR DisGeNET; 115817; -.
DR GeneCards; DHRS1; -.
DR HGNC; HGNC:16445; DHRS1.
DR HPA; ENSG00000157379; Tissue enhanced (esophagus, liver).
DR MIM; 610410; gene.
DR neXtProt; NX_Q96LJ7; -.
DR OpenTargets; ENSG00000157379; -.
DR PharmGKB; PA134914102; -.
DR VEuPathDB; HostDB:ENSG00000157379; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000157797; -.
DR HOGENOM; CLU_010194_14_1_1; -.
DR InParanoid; Q96LJ7; -.
DR OMA; ATVSIWM; -.
DR OrthoDB; 275993at2759; -.
DR PhylomeDB; Q96LJ7; -.
DR TreeFam; TF314146; -.
DR PathwayCommons; Q96LJ7; -.
DR SignaLink; Q96LJ7; -.
DR BioGRID-ORCS; 115817; 6 hits in 1157 CRISPR screens.
DR ChiTaRS; DHRS1; human.
DR EvolutionaryTrace; Q96LJ7; -.
DR GeneWiki; DHRS1; -.
DR GenomeRNAi; 115817; -.
DR Pharos; Q96LJ7; Tdark.
DR PRO; PR:Q96LJ7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96LJ7; Protein.
DR Bgee; ENSG00000157379; Expressed in lower esophagus mucosa and 95 other cell types or tissues.
DR ExpressionAtlas; Q96LJ7; baseline and differential.
DR Genevisible; Q96LJ7; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:RHEA.
DR CDD; cd09763; DHRS1-like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR44147; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 1; 1.
DR PANTHER; PTHR44147:SF2; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER 1; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endoplasmic reticulum; Methylation; NAD;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..313
FT /note="Dehydrogenase/reductase SDR family member 1"
FT /id="PRO_0000054640"
FT REGION 235..313
FT /note="Required for ER localization"
FT /evidence="ECO:0000269|PubMed:30031147"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 21
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99L04"
FT VARIANT 241
FT /note="T -> I (in dbSNP:rs10134537)"
FT /id="VAR_052318"
FT CONFLICT 9
FT /note="V -> A (in Ref. 6; AAH15943)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="P -> L (in Ref. 6; AAH14057)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="K -> R (in Ref. 2; CAD38773)"
FT /evidence="ECO:0000305"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:2QQ5"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:2QQ5"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2QQ5"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:2QQ5"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:2QQ5"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2QQ5"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:2QQ5"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2QQ5"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 161..181
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2QQ5"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:2QQ5"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 225..240
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:2QQ5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2QQ5"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:2QQ5"
SQ SEQUENCE 313 AA; 33909 MW; 832F83FA75D931A3 CRC64;
MAAPMNGQVC VVTGASRGIG RGIALQLCKA GATVYITGRH LDTLRVVAQE AQSLGGQCVP
VVCDSSQESE VRSLFEQVDR EQQGRLDVLV NNAYAGVQTI LNTRNKAFWE TPASMWDDIN
NVGLRGHYFC SVYGARLMVP AGQGLIVVIS SPGSLQYMFN VPYGVGKAAC DKLAADCAHE
LRRHGVSCVS LWPGIVQTEL LKEHMAKEEV LQDPVLKQFK SAFSSAETTE LSGKCVVALA
TDPNILSLSG KVLPSCDLAR RYGLRDVDGR PVQDYLSLSS VLSHVSGLGW LASYLPSFLR
VPKWIIALYT SKF
//
