VDHAP_CHICK
ID VDHAP_CHICK Reviewed; 464 AA.
AC Q90578;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Vitamin D3 hydroxylase-associated protein;
DE Short=VDHAP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Kidney;
RX PubMed=8276793; DOI=10.1016/s0021-9258(17)42331-3;
RA Ettinger R.A., Ismail R., Deluca H.F.;
RT "cDNA cloning and characterization of a vitamin D3 hydroxylase-associated
RT protein.";
RL J. Biol. Chem. 269:176-182(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-21.
RC STRAIN=White leghorn; TISSUE=Kidney;
RX PubMed=1310688; DOI=10.1016/s0021-9258(19)50758-x;
RA Burgos-Trinidad M., Ismail R., Ettinger R.A., Prahl J.M., Deluca H.F.;
RT "Immunopurified 25-hydroxyvitamin D 1 alpha-hydroxylase and 1,25-
RT dihydroxyvitamin D 24-hydroxylase are closely related but distinct
RT enzymes.";
RL J. Biol. Chem. 267:3498-3505(1992).
CC -!- FUNCTION: May have a vitamin D3 hydroxylase regulatory function.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC -!- TISSUE SPECIFICITY: Kidney.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR EMBL; U00694; AAC59645.1; -; mRNA.
DR PIR; A53101; A53101.
DR RefSeq; NP_990307.2; NM_204976.2.
DR AlphaFoldDB; Q90578; -.
DR SMR; Q90578; -.
DR STRING; 9031.ENSGALP00000016939; -.
DR PaxDb; Q90578; -.
DR GeneID; 395824; -.
DR KEGG; gga:395824; -.
DR CTD; 395824; -.
DR VEuPathDB; HostDB:geneid_395824; -.
DR eggNOG; KOG1212; Eukaryota.
DR OrthoDB; 852596at2759; -.
DR PhylomeDB; Q90578; -.
DR SABIO-RK; Q90578; -.
DR PRO; PR:Q90578; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:AgBase.
DR GO; GO:0004040; F:amidase activity; IDA:AgBase.
DR GO; GO:0017064; F:fatty acid amide hydrolase activity; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1310688"
FT CHAIN 2..464
FT /note="Vitamin D3 hydroxylase-associated protein"
FT /id="PRO_0000105268"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 249
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 6..7
FT /note="LW -> PS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="W -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 50891 MW; AA46A129D11B462D CRC64;
MTLERLWQVL DPLWADPRVL SALFCGSAMA VVLLKRLGHR RIQQKMEEAR RARDLALERM
EKAARRFKQE NPGTQTAHIL SLTMVELAEK LKEGSLSPES VLYSYMGKAL EVNREVNCVI
DFIHGCEDQL QKVKQQKEKG LLYGIPVSIK DHIDCKGHVS SAGLVKFLGQ VKEEDSVIVQ
VLKSQGAIPF VKTNIPQTMI NYDCSNLIFG QTLNPLNHQK TPGGSSGGEG ALIAGGGSLL
GIGSDVAGSI RLPSSFCGLC GLKPTGFRIS KLGVISPITG MNSVIGMLGP IARDVDSLAL
CMKALLCEEM FRLDPTVPPI PFDEEVYTSS KPLRIGYYEE DGYFQPSPSM KRAVQQTRKL
LQEAGHTIVP FAPPKIDYVV DELFTRGIFS DGAAHLVDSF KGDIVDPNLK SQFNTYKLPA
LVKRILAIIL KPIYPRIARD LSALCGVGSA KNLWDQHTAV GLPH
