LOCUS       NP_003699                317 aa            linear   PRI 30-APR-2025
DEFINITION  retinol dehydrogenase 16 isoform 1 [Homo sapiens].
ACCESSION   NP_003699
VERSION     NP_003699.3
DBSOURCE    REFSEQ: accession NM_003708.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Hu,P.S., Xia,Q.S., Wu,F., Li,D.K., Qi,Y.J., Hu,Y., Wei,Z.Z.,
            Li,S.S., Tian,N.Y., Wei,Q.F., Shen,L.J., Yin,B., Jiang,T.,
            Yuan,J.G., Qiang,B.Q., Han,W. and Peng,X.Z.
  TITLE     NSPc1 promotes cancer stem cell self-renewal by repressing the
            synthesis of all-trans retinoic acid via targeting RDH16 in
            malignant glioma
  JOURNAL   Oncogene 36 (33), 4706-4718 (2017)
   PUBMED   28394339
  REMARK    GeneRIF: RDH16 is a stemness suppressor that partially rescues stem
            cell-like glioma cells from the NSPc1-induced increase in
            neurosphere formation.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Lapshina,E.A., Belyaeva,O.V., Chumakova,O.V. and Kedishvili,N.Y.
  TITLE     Differential recognition of the free versus bound retinol by human
            microsomal retinol/sterol dehydrogenases: characterization of the
            holo-CRBP dehydrogenase activity of RoDH-4
  JOURNAL   Biochemistry 42 (3), 776-784 (2003)
   PUBMED   12534290
  REMARK    GeneRIF: Characterization of the retinol dehydrogenase activity of
            RoDH-4 identifies it as the enzyme capable of accessing the bound
            form of retinol for retinoic acid production.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Cain,J.M., Zaino,R., Shearer,D., Bennett,R.A., Olt,G. and Weisz,J.
  TITLE     Expression of a retinol dehydrogenase (hRoDH-4), a member of the
            retinol/steroid dehydrogenase family implicated in retinoic acid
            biosynthesis, in normal and neoplastic endometria
  JOURNAL   Am J Obstet Gynecol 186 (4), 675-683 (2002)
   PUBMED   11967490
  REMARK    GeneRIF: In endometrial cancers, hRoDH-4 immunoreactivity was
            markedly reduced.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Chetyrkin,S.V., Belyaeva,O.V., Gough,W.H. and Kedishvili,N.Y.
  TITLE     Characterization of a novel type of human microsomal 3alpha
            -hydroxysteroid dehydrogenase: unique tissue distribution and
            catalytic properties
  JOURNAL   J Biol Chem 276 (25), 22278-22286 (2001)
   PUBMED   11294878
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Jurukovski,V., Markova,N.G., Karaman-Jurukovska,N., Randolph,R.K.,
            Su,J., Napoli,J.L. and Simon,M.
  TITLE     Cloning and characterization of retinol dehydrogenase transcripts
            expressed in human epidermal keratinocytes
  JOURNAL   Mol Genet Metab 67 (1), 62-73 (1999)
   PUBMED   10329026
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Gough,W.H., VanOoteghem,S., Sint,T. and Kedishvili,N.Y.
  TITLE     cDNA cloning and characterization of a new human microsomal
            NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and
            3alpha-hydroxysteroids
  JOURNAL   J Biol Chem 273 (31), 19778-19785 (1998)
   PUBMED   9677409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB209332.1, AF057034.1, AC026120.33 and AW449664.1.
            
            On Jul 2, 2007 this sequence version replaced NP_003699.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF086735.1, SRR5189652.257282.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162895, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398138.5/ ENSP00000381206.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..317
                     /product="retinol dehydrogenase 16 isoform 1"
                     /EC_number="1.1.1.105"
                     /EC_number="1.1.1.315"
                     /EC_number="1.1.1.209"
                     /EC_number="1.1.1.53"
                     /note="microsomal NAD+-dependent retinol dehydrogenase 4;
                     retinol dehydrogenase 16 (all-trans and 13-cis); short
                     chain dehydrogenase/reductase family 9C, member 8;
                     sterol/retinol dehydrogenase; retinol dehydrogenase 16
                     (all-trans); human epidermal retinol dehydrogenase"
                     /calculated_mol_wt=35542
     Region          30..305
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(36,38..39,41,60..62,112..114,162..164,176,180,
                     206..209)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(137,164,176,180)
                     /site_type="active"
                     /db_xref="CDD:187535"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75452.2)"
     CDS             1..317
                     /gene="RDH16"
                     /gene_synonym="hRDH-E; RODH-4; RODH4; SDR9C8"
                     /coded_by="NM_003708.5:147..1100"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41797.1"
                     /db_xref="GeneID:8608"
                     /db_xref="HGNC:HGNC:29674"
                     /db_xref="MIM:620043"
ORIGIN      
        1 mwlylavfvg lyyllhwyre rqvlshlrdk yvfitgcdsg fgkllarqld arglrvlaac
       61 ltekgaeqlr gqtsdrletv tldvtktesv aaaaqwvkec vrdkglwglv nnagislpta
      121 pnelltkqdf vtildvnllg vidvtlsllp lvrrargrvv nvssvmgrvs lfgggycisk
      181 ygveafsdsl rrelsyfgvk vamiepgyfk tavtskerfl ksfleiwdrs spevkeayge
      241 kfvadykksa eqmeqkctqd lslvtncmeh aliachprtr ysagwdakll ylpmsymptf
      301 lvdaimywvs pspakal
//
