PROD_HUMAN
ID PROD_HUMAN Reviewed; 600 AA.
AC O43272; A6NF53; O14680; Q0P507; Q147W8; Q504W1; Q59FI8; Q6NV86; Q9UF13;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Proline dehydrogenase 1, mitochondrial {ECO:0000305};
DE EC=1.5.5.2 {ECO:0000269|PubMed:15662599};
DE AltName: Full=Proline oxidase;
DE AltName: Full=Proline oxidase 2;
DE AltName: Full=p53-induced gene 6 protein;
DE Flags: Precursor;
GN Name=PRODH {ECO:0000312|HGNC:HGNC:9453};
GN Synonyms=PIG6, POX2, PRODH2 {ECO:0000303|PubMed:11891283};
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 3).
RC TISSUE=Brain;
RX PubMed=9385373; DOI=10.1007/s004390050589;
RA Campbell H.D., Webb G.C., Young I.G.;
RT "A human homologue of the Drosophila melanogaster sluggish-A (proline
RT oxidase) gene maps to 22q11.2, and is a candidate gene for type-I
RT hyperprolinaemia.";
RL Hum. Genet. 101:69-74(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Cerebellum, and Kidney;
RX PubMed=10192398; DOI=10.1038/7777;
RA Gogos J.A., Santha M., Takacs Z., Beck K.D., Luine V., Lucas L.R.,
RA Nadler J.V., Karayiorgou M.;
RT "The gene encoding proline dehydrogenase modulates sensorimotor gating in
RT mice.";
RL Nat. Genet. 21:434-439(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY,
RP COFACTOR, VARIANTS VAL-167 AND ARG-521, CHARACTERIZATION OF VARIANTS
RP HYRPRO1 MET-289; ASN-426; MET-427; HIS-431; PRO-441; CYS-453; SER-455;
RP THR-472 AND ARG-521, CHARACTERIZATION OF VARIANTS SCZD4 LEU-406 AND
RP MET-466, AND CHARACTERIZATION OF VARIANTS VAL-167; TRP-185; GLN-185 AND
RP GLU-521.
RC TISSUE=Kidney;
RX PubMed=15662599; DOI=10.1086/428142;
RA Bender H.-U., Almashanu S., Steel G., Hu C.-A., Lin W.-W., Willis A.,
RA Pulver A., Valle D.;
RT "Functional consequences of PRODH missense mutations.";
RL Am. J. Hum. Genet. 76:409-420(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-521.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-600 (ISOFORMS 1/2/3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 444-600, AND INDUCTION BY TP53.
RX PubMed=9305847; DOI=10.1038/38525;
RA Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
RT "A model for p53-induced apoptosis.";
RL Nature 389:300-306(1997).
RN [8]
RP VARIANTS HYRPRO1 MET-289; HIS-431; PRO-441; CYS-453; SER-455; THR-472 AND
RP ARG-521, AND INVOLVEMENT IN HYRPRO1.
RX PubMed=12217952; DOI=10.1093/hmg/11.19.2243;
RA Jacquet H., Raux G., Thibaut F., Hecketsweiler B., Houy E., Demilly C.,
RA Haouzir S., Allio G., Fouldrin G., Drouin V., Bou J., Petit M., Campion D.,
RA Frebourg T.;
RT "PRODH mutations and hyperprolinemia in a subset of schizophrenic
RT patients.";
RL Hum. Mol. Genet. 11:2243-2249(2002).
RN [9]
RP VARIANTS SCZD4 LEU-406; MET-427; PRO-441; CYS-453; MET-466; THR-472 AND
RP ARG-521, AND INVOLVEMENT IN SCZD4.
RX PubMed=11891283; DOI=10.1073/pnas.042700699;
RA Liu H., Heath S.C., Sobin C., Roos J.L., Galke B.L., Blundell M.L.,
RA Lenane M., Robertson B., Wijsman E.M., Rapoport J.L., Gogos J.A.,
RA Karayiorgou M.;
RT "Genetic variation at the 22q11 PRODH2/DGCR6 locus presents an unusual
RT pattern and increases susceptibility to schizophrenia.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3717-3722(2002).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] SER-488.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP VARIANTS ASN-275 AND ASP-444, AND VARIANT HYRPRO1 HIS-431.
RX PubMed=17135275; DOI=10.1093/hmg/ddl443;
RA Raux G., Bumsel E., Hecketsweiler B., van Amelsvoort T., Zinkstok J.,
RA Manouvrier-Hanu S., Fantini C., Breviere G.-M.M., Di Rosa G., Pustorino G.,
RA Vogels A., Swillen A., Legallic S., Bou J., Opolczynski G.,
RA Drouin-Garraud V., Lemarchand M., Philip N., Gerard-Desplanches A.,
RA Carlier M., Philippe A., Nolen M.C., Heron D., Sarda P., Lacombe D.,
RA Coizet C., Alembik Y., Layet V., Afenjar A., Hannequin D., Demily C.,
RA Petit M., Thibaut F., Frebourg T., Campion D.;
RT "Involvement of hyperprolinemia in cognitive and psychiatric features of
RT the 22q11 deletion syndrome.";
RL Hum. Mol. Genet. 16:83-91(2007).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC {ECO:0000269|PubMed:15662599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:132124; EC=1.5.5.2;
CC Evidence={ECO:0000269|PubMed:15662599};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15662599};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43272-4; Sequence=Displayed;
CC Name=2;
CC IsoId=O43272-2; Sequence=VSP_021848;
CC Name=3;
CC IsoId=O43272-1; Sequence=VSP_040848, VSP_040849;
CC -!- TISSUE SPECIFICITY: Expressed in lung, skeletal muscle and brain, to a
CC lesser extent in heart and kidney, and weakly in liver, placenta and
CC pancreas.
CC -!- INDUCTION: During p53/TP53-induced apoptosis.
CC {ECO:0000269|PubMed:9305847}.
CC -!- DISEASE: Hyperprolinemia 1 (HYRPRO1) [MIM:239500]: An inborn error of
CC proline metabolism resulting in elevated levels of proline in the
CC plasma and urine. The disorder is generally benign and most affected
CC individuals are clinically asymptomatic. Some patients, however, have
CC neurologic manifestations, including epilepsy and intellectual
CC disability. Association with certain forms of schizophrenia have been
CC reported. {ECO:0000269|PubMed:12217952, ECO:0000269|PubMed:15662599,
CC ECO:0000269|PubMed:17135275}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Schizophrenia 4 (SCZD4) [MIM:600850]: A complex,
CC multifactorial psychotic disorder or group of disorders characterized
CC by disturbances in the form and content of thought (e.g. delusions,
CC hallucinations), in mood (e.g. inappropriate affect), in sense of self
CC and relationship to the external world (e.g. loss of ego boundaries,
CC withdrawal), and in behavior (e.g bizarre or apparently purposeless
CC behavior). Although it affects emotions, it is distinguished from mood
CC disorders in which such disturbances are primary. Similarly, there may
CC be mild impairment of cognitive function, and it is distinguished from
CC the dementias in which disturbed cognitive function is considered
CC primary. Some patients manifest schizophrenic as well as bipolar
CC disorder symptoms and are often given the diagnosis of schizoaffective
CC disorder. {ECO:0000269|PubMed:11891283, ECO:0000269|PubMed:15662599}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39529.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH68260.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH94736.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH94736.1; Type=Miscellaneous discrepancy; Note=Artifact. Missing internal sequence that doesn't correspond to an exon-intron boundary.; Evidence={ECO:0000305};
CC Sequence=BAD92709.1; Type=Miscellaneous discrepancy; Note=Intron retention. Includes intronic sequence at the 5' end.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U82381; AAB88789.1; -; mRNA.
DR EMBL; AF120278; AAD24775.1; -; mRNA.
DR EMBL; U79754; AAF21464.1; -; mRNA.
DR EMBL; AC007326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068260; AAH68260.1; ALT_FRAME; mRNA.
DR EMBL; BC094736; AAH94736.1; ALT_SEQ; mRNA.
DR EMBL; BC118597; AAI18598.1; -; mRNA.
DR EMBL; BC121809; AAI21810.1; -; mRNA.
DR EMBL; AB209472; BAD92709.1; ALT_SEQ; mRNA.
DR EMBL; AF010310; AAC39529.1; ALT_FRAME; mRNA.
DR CCDS; CCDS13754.1; -. [O43272-4]
DR CCDS; CCDS56223.1; -. [O43272-2]
DR RefSeq; NP_001182155.1; NM_001195226.1.
DR RefSeq; NP_057419.4; NM_016335.4.
DR AlphaFoldDB; O43272; -.
DR BioGRID; 111609; 19.
DR STRING; 9606.ENSP00000481127; -.
DR DrugBank; DB06756; Betaine.
DR DrugBank; DB00172; Proline.
DR iPTMnet; O43272; -.
DR PhosphoSitePlus; O43272; -.
DR SwissPalm; O43272; -.
DR BioMuta; PRODH; -.
DR EPD; O43272; -.
DR jPOST; O43272; -.
DR MassIVE; O43272; -.
DR MaxQB; O43272; -.
DR PaxDb; O43272; -.
DR PeptideAtlas; O43272; -.
DR PRIDE; O43272; -.
DR ProteomicsDB; 48843; -. [O43272-4]
DR ProteomicsDB; 48844; -. [O43272-1]
DR ProteomicsDB; 48845; -. [O43272-2]
DR Antibodypedia; 22803; 320 antibodies from 33 providers.
DR DNASU; 5625; -.
DR Ensembl; ENST00000357068.11; ENSP00000349577.6; ENSG00000100033.17.
DR GeneID; 5625; -.
DR KEGG; hsa:5625; -.
DR UCSC; uc062bjw.1; human. [O43272-4]
DR CTD; 5625; -.
DR DisGeNET; 5625; -.
DR GeneCards; PRODH; -.
DR HGNC; HGNC:9453; PRODH.
DR HPA; ENSG00000100033; Tissue enhanced (skeletal muscle, skin).
DR MalaCards; PRODH; -.
DR MIM; 181500; phenotype.
DR MIM; 239500; phenotype.
DR MIM; 600850; phenotype.
DR MIM; 606810; gene.
DR neXtProt; NX_O43272; -.
DR Orphanet; 419; Hyperprolinemia type 1.
DR PharmGKB; PA33801; -.
DR VEuPathDB; HostDB:ENSG00000100033; -.
DR eggNOG; KOG0186; Eukaryota.
DR InParanoid; O43272; -.
DR OrthoDB; 948528at2759; -.
DR PhylomeDB; O43272; -.
DR TreeFam; TF313544; -.
DR BioCyc; MetaCyc:HS01958-MON; -.
DR BRENDA; 1.5.5.2; 2681.
DR BRENDA; 1.5.99.B2; 2681.
DR PathwayCommons; O43272; -.
DR Reactome; R-HSA-70688; Proline catabolism.
DR SignaLink; O43272; -.
DR SIGNOR; O43272; -.
DR UniPathway; UPA00261; UER00373.
DR BioGRID-ORCS; 5625; 106 hits in 1074 CRISPR screens.
DR ChiTaRS; PRODH; human.
DR GeneWiki; Proline_oxidase; -.
DR GenomeRNAi; 5625; -.
DR Pharos; O43272; Tbio.
DR PRO; PR:O43272; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O43272; protein.
DR Bgee; ENSG00000100033; Expressed in skin of leg and 96 other tissues.
DR ExpressionAtlas; O43272; baseline and differential.
DR Genevisible; O43272; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0004657; F:proline dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019470; P:4-hydroxyproline catabolic process; TAS:BHF-UCL.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; NAS:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006562; P:proline catabolic process; TAS:Reactome.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR GO; GO:0006560; P:proline metabolic process; TAS:ProtInc.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR015659; Proline_oxidase.
DR PANTHER; PTHR13914; PTHR13914; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; FAD; Flavoprotein;
KW Mitochondrion; Oxidoreductase; Proline metabolism; Reference proteome;
KW Schizophrenia; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..600
FT /note="Proline dehydrogenase 1, mitochondrial"
FT /id="PRO_0000025800"
FT REGION 153..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 368
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU79"
FT MOD_RES 486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU79"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021848"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10192398,
FT ECO:0000303|PubMed:9385373"
FT /id="VSP_040848"
FT VAR_SEQ 85..95
FT /note="LLARHEQLLYV -> MLEFVMREWKK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10192398,
FT ECO:0000303|PubMed:9385373"
FT /id="VSP_040849"
FT VARIANT 8
FT /note="P -> L (in dbSNP:rs181332931)"
FT /id="VAR_064883"
FT VARIANT 19
FT /note="Q -> P (moderate reduction of enzymatic activity;
FT dbSNP:rs2008720)"
FT /id="VAR_064884"
FT VARIANT 30
FT /note="P -> S (in dbSNP:rs3815655)"
FT /id="VAR_064885"
FT VARIANT 58
FT /note="A -> T (in dbSNP:rs146648839)"
FT /id="VAR_064886"
FT VARIANT 167
FT /note="A -> V (may be a risk factor for schizophrenia;
FT moderate reduction of enzymatic activity;
FT dbSNP:rs761544165)"
FT /evidence="ECO:0000269|PubMed:15662599"
FT /id="VAR_029563"
FT VARIANT 185
FT /note="R -> Q (mild decrease of enzymatic activity;
FT dbSNP:rs11913840 and dbSNP:rs386819653)"
FT /evidence="ECO:0000269|PubMed:15662599"
FT /id="VAR_029564"
FT VARIANT 185
FT /note="R -> W (moderate reduction of enzymatic activity;
FT dbSNP:rs4819756)"
FT /evidence="ECO:0000269|PubMed:15662599"
FT /id="VAR_029565"
FT VARIANT 275
FT /note="T -> N (in dbSNP:rs5747933)"
FT /evidence="ECO:0000269|PubMed:17135275"
FT /id="VAR_029874"
FT VARIANT 289
FT /note="L -> M (in HYRPRO1; mild decrease of enzymatic
FT activity; dbSNP:rs137852934)"
FT /evidence="ECO:0000269|PubMed:12217952,
FT ECO:0000269|PubMed:15662599"
FT /id="VAR_029566"
FT VARIANT 406
FT /note="P -> L (in SCZD4; may be associated with disease
FT susceptibility; strongly reduced enzymatic activity;
FT dbSNP:rs3970555)"
FT /evidence="ECO:0000269|PubMed:11891283,
FT ECO:0000269|PubMed:15662599"
FT /id="VAR_029567"
FT VARIANT 426
FT /note="D -> N (in HYRPRO1; moderate reduction of enzymatic
FT activity)"
FT /evidence="ECO:0000269|PubMed:15662599"
FT /id="VAR_029568"
FT VARIANT 427
FT /note="V -> M (in HYRPRO1 and SCZD4; may be associated with
FT disease susceptibility; moderate reduction of enzymatic
FT activity; dbSNP:rs2238731)"
FT /evidence="ECO:0000269|PubMed:11891283,
FT ECO:0000269|PubMed:15662599"
FT /id="VAR_029569"
FT VARIANT 431
FT /note="R -> H (in HYRPRO1; moderate reduction of enzymatic
FT activity; dbSNP:rs2904552)"
FT /evidence="ECO:0000269|PubMed:12217952,
FT ECO:0000269|PubMed:15662599, ECO:0000269|PubMed:17135275"
FT /id="VAR_029570"
FT VARIANT 441
FT /note="L -> P (in HYRPRO1 and SCZD4; may be associated with
FT disease susceptibility; strongly reduced enzymatic
FT activity; dbSNP:rs2904551)"
FT /evidence="ECO:0000269|PubMed:11891283,
FT ECO:0000269|PubMed:12217952, ECO:0000269|PubMed:15662599"
FT /id="VAR_029571"
FT VARIANT 444
FT /note="G -> D (in dbSNP:rs765090516)"
FT /evidence="ECO:0000269|PubMed:17135275"
FT /id="VAR_029875"
FT VARIANT 453
FT /note="R -> C (in HYRPRO1 and SCZD4; may be associated with
FT disease susceptibility; strongly reduced enzymatic
FT activity; dbSNP:rs3970559)"
FT /evidence="ECO:0000269|PubMed:11891283,
FT ECO:0000269|PubMed:12217952, ECO:0000269|PubMed:15662599"
FT /id="VAR_029572"
FT VARIANT 455
FT /note="A -> S (in HYRPRO1; mild decrease of enzymatic
FT activity; dbSNP:rs1807467)"
FT /evidence="ECO:0000269|PubMed:12217952,
FT ECO:0000269|PubMed:15662599"
FT /id="VAR_029573"
FT VARIANT 466
FT /note="T -> M (in SCZD4; may be associated with disease
FT susceptibility; strongly reduced affinity for FAD; strongly
FT reduced enzymatic activity; dbSNP:rs2870984)"
FT /evidence="ECO:0000269|PubMed:11891283,
FT ECO:0000269|PubMed:15662599"
FT /id="VAR_029574"
FT VARIANT 472
FT /note="A -> T (in HYRPRO1 and SCZD4; associated with
FT disease susceptibility; mild decrease of enzymatic
FT activity; dbSNP:rs2870983)"
FT /evidence="ECO:0000269|PubMed:11891283,
FT ECO:0000269|PubMed:12217952, ECO:0000269|PubMed:15662599"
FT /id="VAR_029575"
FT VARIANT 488
FT /note="N -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs139903009)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036566"
FT VARIANT 521
FT /note="Q -> E (strongly reduced enzymatic activity;
FT dbSNP:rs193919334)"
FT /evidence="ECO:0000269|PubMed:15662599"
FT /id="VAR_029576"
FT VARIANT 521
FT /note="Q -> R (in HYRPRO1 and SCZD4; may be associated with
FT disease susceptibility; enhanced enzymatic activity;
FT dbSNP:rs450046)"
FT /evidence="ECO:0000269|PubMed:11891283,
FT ECO:0000269|PubMed:12217952, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15662599"
FT /id="VAR_029577"
FT CONFLICT 144
FT /note="Y -> F (in Ref. 5; AAH94736)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="T -> S (in Ref. 1; AAB88789)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="P -> H (in Ref. 5; AAH68260)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="R -> G (in Ref. 3; AAF21464)"
FT /evidence="ECO:0000305"
FT CONFLICT 455..456
FT /note="AE -> Q (in Ref. 7; AAC39529)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="L -> F (in Ref. 6; BAD92709)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="R -> K (in Ref. 7; AAC39529)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="F -> L (in Ref. 5; AAH68260)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 68002 MW; 249E98A0A5BB8027 CRC64;
MALRRALPAL RPCIPRFVQL STAPASREQP AAGPAAVPGG GSATAVRPPV PAVDFGNAQE
AYRSRRTWEL ARSLLVLRLC AWPALLARHE QLLYVSRKLL GQRLFNKLMK MTFYGHFVAG
EDQESIQPLL RHYRAFGVSA ILDYGVEEDL SPEEAEHKEM ESCTSAAERD GSGTNKRDKQ
YQAHRAFGDR RNGVISARTY FYANEAKCDS HMETFLRCIE ASGRVSDDGF IAIKLTALGR
PQFLLQFSEV LAKWRCFFHQ MAVEQGQAGL AAMDTKLEVA VLQESVAKLG IASRAEIEDW
FTAETLGVSG TMDLLDWSSL IDSRTKLSKH LVVPNAQTGQ LEPLLSRFTE EEELQMTRML
QRMDVLAKKA TEMGVRLMVD AEQTYFQPAI SRLTLEMQRK FNVEKPLIFN TYQCYLKDAY
DNVTLDVELA RREGWCFGAK LVRGAYLAQE RARAAEIGYE DPINPTYEAT NAMYHRCLDY
VLEELKHNAK AKVMVASHNE DTVRFALRRM EELGLHPADH QVYFGQLLGM CDQISFPLGQ
AGYPVYKYVP YGPVMEVLPY LSRRALENSS LMKGTHRERQ LLWLELLRRL RTGNLFHRPA
