ID A0A2K6SLW2_SAIBB Unreviewed; 544 AA.
AC A0A2K6SLW2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN Name=P4HA3 {ECO:0000313|Ensembl:ENSSBOP00000008380.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000008380.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000008380.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC proteins. {ECO:0000256|ARBA:ARBA00002035}.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the P4HA family.
CC {ECO:0000256|ARBA:ARBA00006511}.
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DR STRING; 39432.ENSSBOP00000008380; -.
DR Ensembl; ENSSBOT00000025140.1; ENSSBOP00000008380.1; ENSSBOG00000021114.1.
DR GeneTree; ENSGT00940000158967; -.
DR OMA; DVYMPAV; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR Gene3D; 6.10.140.1460; -; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR013547; Pro_4_hyd_alph_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF223; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-3; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 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:UP000233220}.
FT DOMAIN 422..529
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 544 AA; 61246 MW; DC511978F60153B0 CRC64;
XXXXXXXXXX LAVLVLGTGD PERAAARGDT FSALTSVARA LAPERQLLGL LRRYLREEEA
RLRDLTRFYD KVLSLHEDST TPVGNPLLAF TLIKRLQSDW RNVVHSLEAS ENIRALKDGY
EKVEQDLPAF EDLEGAARAL MRLQDVYMLN VKGLARGVFQ RVTGSAITDL YSPKRLFSLT
GDDCFQVGKV AYDMGDYYHA IPWLEEAVSL FRGSYGEWKT EDEASLEDAL DHLAFACFQA
GNVSCALSLS REFLLYSPDN KRMARNVLKY ERLLAESPNQ VVAEAVIQRP NIPHLQTRDT
YEGLCQTLGS QPTLYQIPSL YCSYEINSNP YLLLQPIQKE VLHLEPYIAL YHDFVSDSEA
QKIRELAEPW LQRSVVASGE KQLQVEYRIS KSAWLKDTVD PMLVTLNHRI AALTGLDVRP
PYAEYLQVVN YGIGGHYEPH FDHATSPSSP LYRMKSGNRV ATFMIYLSSV EAGGATAFIY
ANLSVPVVKN AALFWWNLHR SGEGDSDTLH AGCPVLVGNK WVANKWIHEY GQEFRRPCSS
SPED
//
