Reviewed, UniProtKB/Swiss-Prot Q3V1T4 (P3H1_MOUSE)

Names and origin

Protein names

Recommended name:
    Prolyl 3-hydroxylase 1
    EC=1.14.11.7
Alternative name(s):
    Leucine- and proline-enriched proteoglycan 1
      Short name=Leprecan-1
    Growth suppressor 1

Gene names

Name:	Lepre1
Synonyms:	Gros1, P3h1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	739 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts By similarity.
Catalytic activity	Procollagen L-proline + 2-oxoglutarate + O(2) = procollagen trans-3-hydroxy-L-proline + succinate + CO(2).
Cofactor	Iron By similarity. Ascorbate By similarity.
Subcellular location	Endoplasmic reticulumBy similarity. Secreted › extracellular space › extracellular matrixBy similarity. Note= Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG).
Post-translational modification	O-glycosylated; chondroitin sulfate By similarity.
Sequence similarities	Belongs to the leprecan family. Contains 1 PKHD (prolyl/lysyl hydroxylase) domain. Contains 4 TPR repeats.
Sequence caution	The sequence BAB27041.1 differs from that shown. Reason: Frameshift at position 707. The sequence BAE21065.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Signal TPR repeat
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	cell growth Ref.1 Inferred from direct assay. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: InterPro nucleus Ref.1 Inferred from direct assay. Source: MGI plasma membrane Ref.1 Traceable author statement. Source: MGI proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW procollagen-proline 3-dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3V1T4-1)

Also known as: GROS1-L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q3V1T4-2)

Also known as: GROS1-S;

The sequence of this isoform differs from the canonical sequence as follows:
     540-543: MYYN → TALQ
     544-739: Missing.

Isoform 3 (identifier: Q3V1T4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-179: Missing.

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 739	714	Prolyl 3-hydroxylase 1		PRO_0000240353
Regions
	Repeat	36 – 69	34	TPR 1
	Repeat	146 – 179	34	TPR 2
	Repeat	208 – 241	34	TPR 3
	Repeat	304 – 337	34	TPR 4
	Domain	472 – 680	209	PKHD
	Coiled coil	404 – 442	39	Potential
	Motif	736 – 739	4	Prevents secretion from ER Potential
Sites
	Active site	672	1	By similarity
	Metal binding	590	1	Iron
	Metal binding	592	1	Iron
	Metal binding	662	1	Iron
Amino acid modifications
	Glycosylation	319	1	N-linked (GlcNAc...) Potential
	Glycosylation	470	1	N-linked (GlcNAc...) Potential
	Glycosylation	543	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 179	179	Missing in isoform 3.		VSP_019349
	Alternative sequence	540 – 543	4	MYYN → TALQ in isoform 2.		VSP_019350
	Alternative sequence	544 – 739	196	Missing in isoform 2.		VSP_019351
Experimental info
	Sequence conflict	4 – 25	22	SERRL…LRVAA → TKGGCWHDASGRRRRRLTGC G in AAF04806 and AAF04807. Ref.1
	Sequence conflict	50	1	G → R in AAF04806 and AAF04807. Ref.1
	Sequence conflict	371 – 372	2	RS → PN in AAF04806 and AAF04807. Ref.1
	Sequence conflict	403	1	P → T in BAE21065. Ref.2
	Sequence conflict	420	1	Missing in BAC26962. Ref.2
	Sequence conflict	484	1	D → N in BAE35138. Ref.2
	Sequence conflict	569	1	L → F in AAF04806. Ref.1
	Sequence conflict	589	1	V → D in BAE21065. Ref.2
	Sequence conflict	601	1	L → F in AAF04806. Ref.1
	Sequence conflict	614	1	D → E in AAF04806. Ref.1
	Sequence conflict	685	1	H → Q in BAC26962. Ref.2
	Sequence conflict	716	1	D → G in BAE35138. Ref.2
	Sequence conflict	716	1	D → G in AAH24047. Ref.3
	Sequence conflict	727 – 739	13	SLSDR…HKDEL → FLHGATVLGVGIA in AAF04806. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GROS1-L) [UniParc]. Last modified June 27, 2006. Version 2. Checksum: 3484AE68E80B68E8	FASTA	739	83,651
	10 20 30 40 50 60 MAVSERRLLA AMLAVAAAAA LRVAAESEPG WDVAAPDLLY AEGTAAYSRG DWPGVVLNME 70 80 90 100 110 120 RALRSRAALR ALRLRCRTRC ATELPWAPDL DLGPDPSLSQ DPGAAALHDL RFFGAVLRRA 130 140 150 160 170 180 ACLRRCLGPP SAHLLSEELD LEFNKRSPYN YLQVAYFKIN KLEKAVAAAH TFFVGNPEHM 190 200 210 220 230 240 EMRQNLDYYQ TMSGVKEADF RDLEAKPHMH EFRLGVRLYS EEKPQEAVPH LEAALQEYFV 250 260 270 280 290 300 ADEECRALCE GPYDYDGYNY LDYSADLFQA ITDHYVQVLN CKQNCVTELA SHPSREKPFE 310 320 330 340 350 360 DFLPSHYNYL QFAYYNIGNY TQAIECAKTY LLFFPNDEVM HQNLAYYTAM LGEEEASSIS 370 380 390 400 410 420 PRENAEEYRR RSLLEKELLF FAYDIFGIPF VDPDSWTPEE VIPKRLQEKQ KSERETAVRI 430 440 450 460 470 480 SQEIGNLMKE IETLVEEKTK ESLDVSRLTR EGGPLLYEGI SLTMNSKVLN GSQRVVMDGV 490 500 510 520 530 540 ISDDECQELQ RLTNAAATSG DGYRGQTSPH TPNEKFYGVT VLKALKLGQE GKVPLQSARM 550 560 570 580 590 600 YYNVTEKVRR VMESYFRLDT PLYFSYSHLV CRTAIEESQA ERKDSSHPVH VDNCILNAEA 610 620 630 640 650 660 LMCIKEPPAY TFRDYSAILY LNGDFDGGNF YFTELDAKTV TAEVQPQCGR AVGFSSGTEN 670 680 690 700 710 720 PHGVKAVTRG QRCAIALWFT LDPRHSERDR VQADDLVKML FSPEEVDLPQ EQPLPDQQGS 730 PEPGEESLSD RGSLHKDEL
	Isoform 2 (GROS1-S) [UniParc]. Checksum: 2166EB32EC38A766		543	61,397
	10 20 30 40 50 60 MAVSERRLLA AMLAVAAAAA LRVAAESEPG WDVAAPDLLY AEGTAAYSRG DWPGVVLNME 70 80 90 100 110 120 RALRSRAALR ALRLRCRTRC ATELPWAPDL DLGPDPSLSQ DPGAAALHDL RFFGAVLRRA 130 140 150 160 170 180 ACLRRCLGPP SAHLLSEELD LEFNKRSPYN YLQVAYFKIN KLEKAVAAAH TFFVGNPEHM 190 200 210 220 230 240 EMRQNLDYYQ TMSGVKEADF RDLEAKPHMH EFRLGVRLYS EEKPQEAVPH LEAALQEYFV 250 260 270 280 290 300 ADEECRALCE GPYDYDGYNY LDYSADLFQA ITDHYVQVLN CKQNCVTELA SHPSREKPFE 310 320 330 340 350 360 DFLPSHYNYL QFAYYNIGNY TQAIECAKTY LLFFPNDEVM HQNLAYYTAM LGEEEASSIS 370 380 390 400 410 420 PRENAEEYRR RSLLEKELLF FAYDIFGIPF VDPDSWTPEE VIPKRLQEKQ KSERETAVRI 430 440 450 460 470 480 SQEIGNLMKE IETLVEEKTK ESLDVSRLTR EGGPLLYEGI SLTMNSKVLN GSQRVVMDGV 490 500 510 520 530 540 ISDDECQELQ RLTNAAATSG DGYRGQTSPH TPNEKFYGVT VLKALKLGQE GKVPLQSART ALQ
	Isoform 3 [UniParc]. Checksum: 673B7643F80A1388		560	64,102
	10 20 30 40 50 60 MEMRQNLDYY QTMSGVKEAD FRDLEAKPHM HEFRLGVRLY SEEKPQEAVP HLEAALQEYF 70 80 90 100 110 120 VADEECRALC EGPYDYDGYN YLDYSADLFQ AITDHYVQVL NCKQNCVTEL ASHPSREKPF 130 140 150 160 170 180 EDFLPSHYNY LQFAYYNIGN YTQAIECAKT YLLFFPNDEV MHQNLAYYTA MLGEEEASSI 190 200 210 220 230 240 SPRENAEEYR RRSLLEKELL FFAYDIFGIP FVDPDSWTPE EVIPKRLQEK QKSERETAVR 250 260 270 280 290 300 ISQEIGNLMK EIETLVEEKT KESLDVSRLT REGGPLLYEG ISLTMNSKVL NGSQRVVMDG 310 320 330 340 350 360 VISDDECQEL QRLTNAAATS GDGYRGQTSP HTPNEKFYGV TVLKALKLGQ EGKVPLQSAR 370 380 390 400 410 420 MYYNVTEKVR RVMESYFRLD TPLYFSYSHL VCRTAIEESQ AERKDSSHPV HVDNCILNAE 430 440 450 460 470 480 ALMCIKEPPA YTFRDYSAIL YLNGDFDGGN FYFTELDAKT VTAEVQPQCG RAVGFSSGTE 490 500 510 520 530 540 NPHGVKAVTR GQRCAIALWF TLDPRHSERD RVQADDLVKM LFSPEEVDLP QEQPLPDQQG 550 560 SPEPGEESLS DRGSLHKDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan." Kaul S.C., Sugihara T., Yoshida A., Nomura H., Wadhwa R. Oncogene 19:3576-3583(2000) [PubMed: 10951563] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Strain: CD-1/ICR. Tissue: Fibroblast and Testis.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Strain: C57BL/6J. Tissue: Embryonic stem cell, Pituitary and Placenta.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Mammary tumor.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF165163 mRNA. Translation: AAF04806.1. Sequence problems. AF165164 mRNA. Translation: AAF04807.1. Sequence problems. AK010578 mRNA. Translation: BAB27041.1. Frameshift. AK030436 mRNA. Translation: BAC26962.1. AK132262 mRNA. Translation: BAE21065.1. Sequence problems. AK159505 mRNA. Translation: BAE35138.1. BC024047 mRNA. Translation: AAH24047.1.
RefSeq	NP_001035874.1. NP_062756.2. NP_062757.2.
UniGene	Mm.27961
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q3V1T4.
Genome annotation databases
Ensembl	ENSMUSG00000028641. Mus musculus. [Contig view]
GeneID	56401.
KEGG	mmu:56401.
Organism-specific databases
MGI	MGI:1888921. Lepre1.
Phylogenomic databases
HOVERGEN	Q3V1T4.
Gene expression databases
ArrayExpress	Q3V1T4.
CleanEx	MM_LEPRE1.
GermOnline	ENSMUSG00000028641. Mus musculus.
Family and domain databases
InterPro	IPR005123. 2OG-FeII_Oase. IPR000886. ER_targeting_sequence. IPR006620. Pro_4_hyd_alph. IPR013026. TPR_region. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	312512.
SOURCE	Search...

Entry information

Entry name

P3H1_MOUSE

Accession

Primary (citable) accession number: Q3V1T4
Secondary accession number(s): Q3TWX8 , Q8BSV2, Q8CFL3, Q9CWK5, Q9QZT6, Q9QZT7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	June 27, 2006
Last modified:	November 25, 2008
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)