P3H1_MOUSE
ID P3H1_MOUSE Reviewed; 739 AA.
AC Q3V1T4; A2A7Q4; A6PW85; Q3TWX8; Q8BSV2; Q8CFL3; Q9CWK5; Q9QZT6; Q9QZT7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Prolyl 3-hydroxylase 1 {ECO:0000312|MGI:MGI:1888921};
DE EC=1.14.11.7;
DE AltName: Full=Growth suppressor 1 {ECO:0000303|PubMed:10951563};
DE AltName: Full=Leucine- and proline-enriched proteoglycan 1 {ECO:0000250|UniProtKB:Q9R1J8};
DE Short=Leprecan-1 {ECO:0000250|UniProtKB:Q9R1J8};
DE Flags: Precursor;
GN Name=P3h1 {ECO:0000312|MGI:MGI:1888921};
GN Synonyms=Gros1 {ECO:0000303|PubMed:10951563},
GN Lepre1 {ECO:0000250|UniProtKB:Q9R1J8};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=CD-1/ICR; TISSUE=Fibroblast, and Testis;
RX PubMed=10951563; DOI=10.1038/sj.onc.1203696;
RA Kaul S.C., Sugihara T., Yoshida A., Nomura H., Wadhwa R.;
RT "Gros1, a potential growth suppressor on chromosome 1: its identity to
RT basement membrane-associated proteoglycan, leprecan.";
RL Oncogene 19:3576-3583(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Pituitary, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan
CC (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-
CC translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences
CC in collagens, especially types IV and V. May be involved in the
CC secretory pathway of cells. Has growth suppressive activity in
CC fibroblasts (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}. Secreted, extracellular space, extracellular matrix
CC {ECO:0000250}. Note=Secreted into the extracellular matrix as a
CC chondroitin sulfate proteoglycan (CSPG).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=GROS1-L;
CC IsoId=Q3V1T4-1; Sequence=Displayed;
CC Name=2; Synonyms=GROS1-S;
CC IsoId=Q3V1T4-2; Sequence=VSP_019350, VSP_019351;
CC Name=3;
CC IsoId=Q3V1T4-3; Sequence=VSP_019349;
CC -!- PTM: O-glycosylated; chondroitin sulfate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27041.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE21065.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF165163; AAF04806.1; ALT_SEQ; mRNA.
DR EMBL; AF165164; AAF04807.1; ALT_SEQ; mRNA.
DR EMBL; AK010578; BAB27041.1; ALT_FRAME; mRNA.
DR EMBL; AK030436; BAC26962.1; -; mRNA.
DR EMBL; AK132262; BAE21065.1; ALT_SEQ; mRNA.
DR EMBL; AK159505; BAE35138.1; -; mRNA.
DR EMBL; AL606975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024047; AAH24047.1; -; mRNA.
DR CCDS; CCDS38859.1; -. [Q3V1T4-1]
DR CCDS; CCDS38860.1; -. [Q3V1T4-3]
DR RefSeq; NP_001035874.1; NM_001042411.1. [Q3V1T4-3]
DR RefSeq; NP_001273077.1; NM_001286148.1.
DR RefSeq; NP_062756.2; NM_019782.3.
DR RefSeq; NP_062757.2; NM_019783.2. [Q3V1T4-1]
DR AlphaFoldDB; Q3V1T4; -.
DR SMR; Q3V1T4; -.
DR BioGRID; 207954; 2.
DR STRING; 10090.ENSMUSP00000099723; -.
DR GlyGen; Q3V1T4; 3 sites.
DR iPTMnet; Q3V1T4; -.
DR PhosphoSitePlus; Q3V1T4; -.
DR EPD; Q3V1T4; -.
DR MaxQB; Q3V1T4; -.
DR PaxDb; Q3V1T4; -.
DR PeptideAtlas; Q3V1T4; -.
DR PRIDE; Q3V1T4; -.
DR ProteomicsDB; 294293; -. [Q3V1T4-1]
DR ProteomicsDB; 294294; -. [Q3V1T4-2]
DR ProteomicsDB; 294295; -. [Q3V1T4-3]
DR Antibodypedia; 32239; 305 antibodies from 23 providers.
DR DNASU; 56401; -.
DR Ensembl; ENSMUST00000081606; ENSMUSP00000080312; ENSMUSG00000028641. [Q3V1T4-3]
DR Ensembl; ENSMUST00000121111; ENSMUSP00000112504; ENSMUSG00000028641. [Q3V1T4-1]
DR GeneID; 56401; -.
DR KEGG; mmu:56401; -.
DR UCSC; uc008ulq.1; mouse. [Q3V1T4-1]
DR CTD; 64175; -.
DR MGI; MGI:1888921; P3h1.
DR VEuPathDB; HostDB:ENSMUSG00000028641; -.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000158725; -.
DR HOGENOM; CLU_017820_1_0_1; -.
DR InParanoid; Q3V1T4; -.
DR OrthoDB; 660619at2759; -.
DR BRENDA; 1.14.11.7; 3474.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 56401; 1 hit in 75 CRISPR screens.
DR ChiTaRS; P3h1; mouse.
DR PRO; PR:Q3V1T4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3V1T4; protein.
DR Bgee; ENSMUSG00000028641; Expressed in humerus cartilage element and 227 other tissues.
DR ExpressionAtlas; Q3V1T4; baseline and differential.
DR Genevisible; Q3V1T4; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; ISO:MGI.
DR GO; GO:0060348; P:bone development; ISO:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0032963; P:collagen metabolic process; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:MGI.
DR GO; GO:1901874; P:negative regulation of post-translational protein modification; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0018126; P:protein hydroxylation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0030278; P:regulation of ossification; IMP:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; ISO:MGI.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR039837; P3H1.
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; PTHR14049; 1.
DR PANTHER; PTHR14049:SF5; PTHR14049:SF5; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Dioxygenase; Endoplasmic reticulum;
KW Extracellular matrix; Glycoprotein; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Secreted; Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..739
FT /note="Prolyl 3-hydroxylase 1"
FT /id="PRO_0000240353"
FT REPEAT 36..69
FT /note="TPR 1"
FT REPEAT 146..179
FT /note="TPR 2"
FT REPEAT 208..241
FT /note="TPR 3"
FT REPEAT 304..337
FT /note="TPR 4"
FT DOMAIN 567..681
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 702..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..442
FT /evidence="ECO:0000255"
FT MOTIF 736..739
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 672
FT /evidence="ECO:0000250"
FT BINDING 590
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 592
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 662
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..179
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019349"
FT VAR_SEQ 540..543
FT /note="MYYN -> TALQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10951563"
FT /id="VSP_019350"
FT VAR_SEQ 544..739
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10951563"
FT /id="VSP_019351"
FT CONFLICT 4..25
FT /note="SERRLLAAMLAVAAAAALRVAA -> TKGGCWHDASGRRRRRLTGCG (in
FT Ref. 1; AAF04806/AAF04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="G -> R (in Ref. 1; AAF04806/AAF04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..372
FT /note="RS -> PN (in Ref. 1; AAF04806/AAF04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="P -> T (in Ref. 2; BAE21065)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="Missing (in Ref. 2; BAC26962)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="D -> N (in Ref. 2; BAE35138)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="L -> F (in Ref. 1; AAF04806)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="V -> D (in Ref. 2; BAE21065)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="L -> F (in Ref. 1; AAF04806)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="D -> E (in Ref. 1; AAF04806)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="H -> Q (in Ref. 2; BAC26962)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="D -> G (in Ref. 2; BAE35138 and 3; AAH24047)"
FT /evidence="ECO:0000305"
FT CONFLICT 727..739
FT /note="SLSDRGSLHKDEL -> FLHGATVLGVGIA (in Ref. 1;
FT AAF04806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 83651 MW; 3484AE68E80B68E8 CRC64;
MAVSERRLLA AMLAVAAAAA LRVAAESEPG WDVAAPDLLY AEGTAAYSRG DWPGVVLNME
RALRSRAALR ALRLRCRTRC ATELPWAPDL DLGPDPSLSQ DPGAAALHDL RFFGAVLRRA
ACLRRCLGPP SAHLLSEELD LEFNKRSPYN YLQVAYFKIN KLEKAVAAAH TFFVGNPEHM
EMRQNLDYYQ TMSGVKEADF RDLEAKPHMH EFRLGVRLYS EEKPQEAVPH LEAALQEYFV
ADEECRALCE GPYDYDGYNY LDYSADLFQA ITDHYVQVLN CKQNCVTELA SHPSREKPFE
DFLPSHYNYL QFAYYNIGNY TQAIECAKTY LLFFPNDEVM HQNLAYYTAM LGEEEASSIS
PRENAEEYRR RSLLEKELLF FAYDIFGIPF VDPDSWTPEE VIPKRLQEKQ KSERETAVRI
SQEIGNLMKE IETLVEEKTK ESLDVSRLTR EGGPLLYEGI SLTMNSKVLN GSQRVVMDGV
ISDDECQELQ RLTNAAATSG DGYRGQTSPH TPNEKFYGVT VLKALKLGQE GKVPLQSARM
YYNVTEKVRR VMESYFRLDT PLYFSYSHLV CRTAIEESQA ERKDSSHPVH VDNCILNAEA
LMCIKEPPAY TFRDYSAILY LNGDFDGGNF YFTELDAKTV TAEVQPQCGR AVGFSSGTEN
PHGVKAVTRG QRCAIALWFT LDPRHSERDR VQADDLVKML FSPEEVDLPQ EQPLPDQQGS
PEPGEESLSD RGSLHKDEL
