ID   A0A2K5YVL7_MANLE        Unreviewed;       736 AA.
AC   A0A2K5YVL7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=procollagen-proline 3-dioxygenase {ECO:0000256|ARBA:ARBA00012262};
DE            EC=1.14.11.7 {ECO:0000256|ARBA:ARBA00012262};
GN   Name=P3H1 {ECO:0000313|Ensembl:ENSMLEP00000019606.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000019606.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000019606.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC         trans-3-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:22872, Rhea:RHEA-
CC         COMP:11676, Rhea:RHEA-COMP:11678, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; EC=1.14.11.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024148};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SIMILARITY: Belongs to the leprecan family.
CC       {ECO:0000256|ARBA:ARBA00006487}.
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DR   RefSeq; XP_011857136.1; XM_012001746.1.
DR   AlphaFoldDB; A0A2K5YVL7; -.
DR   Ensembl; ENSMLET00000043096.1; ENSMLEP00000019606.1; ENSMLEG00000034003.1.
DR   GeneID; 105555039; -.
DR   KEGG; mleu:105555039; -.
DR   CTD; 64175; -.
DR   GeneTree; ENSGT00940000158725; -.
DR   OMA; HTPSEMF; -.
DR   OrthoDB; 5398065at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032963; P:collagen metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR039575; P3H.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR14049; LEPRECAN 1; 1.
DR   PANTHER; PTHR14049:SF5; PROLYL 3-HYDROXYLASE 1; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..736
FT                   /note="procollagen-proline 3-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014356253"
FT   DOMAIN          564..678
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          699..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   736 AA;  83179 MW;  2F34F9DD7B500309 CRC64;
     MAARALKLLS TLLAVVAAAS QAEVESEAGW GVVTPDLLFA EGTAAYARGD WPGVVLSMER
     ALRSRAALRA LRLRCRTRCA ADFPWELDPE SLPSPAQASG AAALRDLSFF GGLLRRAACL
     RGCLGPPAAH SLSEEMELEF RKRSPYNYLQ VAYFKINKLE KAVAAAHTFF VGNPEHMEMR
     QNLDYYQTMS GVKEADFKDL ETQPHMQEFR LGVRLYSEEQ PQEAVPHLEA ALHEYFVAYE
     ECHALCEGPY DYDGYNYLEY NADLFQAITD HYIQVLSCKQ NCVTELASHP SREKPFEDFL
     PSHYNYLQFA YYNIGNYTQA VECAKTYLLF FPNDEVMNQN LAYYAAMLGE EHARSIGPRE
     SAKEYRQRSL LEKELLFFAY DVFGIPFVDP DSWTPEEVIP KRLQEKQKSE RETAVRISQE
     IGNLMKEIET LVEEKTKESL DVSRLTREGG PLLYEGISLT MNSRLLNGSQ RVVMDGVISD
     HECQELQRLT NVAATSGDGY RGQTSPHTPN EKFYGVTVFK ALKLGQEGKV PLQSAHLYYN
     VTEKVRRIME SYFRLDTPLY FSYSHLVCRT AIEEVQAERK DDSHPVHVDN CILNAETLVC
     VKEPPAYTFR DYSAILYLNG DFDGGNFYFT ELDAKTVTAE VQPQCGRAVG FSSGTENPHG
     VKAVTRGQRC AIALWFTLDP RHSERDRVQA DDLVKMLFSP EEMDLSQEQP LDAQQGPPEP
     AQESLSGSES KPKDEL
//