[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). STRAIN=CD-1/ICR; TISSUE=Fibroblast, and Testis; DOI=10.1038/sj.onc.1203696; PubMed=10951563 [NCBI, ExPASy, EBI, Israel, Japan] Kaul S.C., Sugihara T., Yoshida A., Nomura H., Wadhwa R.; "Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan."; Oncogene 19:3576-3583(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Pituitary, and Placenta; DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The transcriptional landscape of the mammalian genome."; Science 309:1559-1563(2005).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). STRAIN=FVB/N; TISSUE=Mammary tumor; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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 + O₂ = procollagen trans-3-hydroxy-L-proline + succinate + CO₂.
COFACTOR: Iron (By similarity).
COFACTOR: Ascorbate (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). Secreted, extracellular space, extracellular matrix (By similarity). Note=Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG).

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	GROS1-L
Isoform ID	Q3V1T4-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	GROS1-S
Isoform ID	Q3V1T4-2
Features which should be applied to build the isoform sequence: VSP_019350, VSP_019351.

Name	3
Isoform ID	Q3V1T4-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_019349.

PTM: O-glycosylated; chondroitin sulfate (By similarity).
SIMILARITY: Belongs to the leprecan family.
SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
SIMILARITY: Contains 4 TPR repeats.
SEQUENCE CAUTION:
- Sequence=BAB27041.1; Type=Frameshift; Positions=707;
- Sequence=BAE21065.1; Type=Miscellaneous discrepancy; Note=Intron retention

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF165163; AAF04806.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF165164; AAF04807.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK010578; BAB27041.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK030436; BAC26962.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK132262; BAE21065.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK159505; BAE35138.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024047; AAH24047.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001035874.1; -.
NP_062756.2; -.
NP_062757.2; -.

UniGene

Mm.27961

3D structure databases

ModBase

Q3V1T4.

Organism-specific databases

MGI

MGI:1888921; Lepre1.

Gene expression databases

ArrayExpress

Q3V1T4; -.

CleanEx

MM_LEPRE1; -.

GermOnline

ENSMUSG00000028641; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from MGI).
GO:0005886;	Cellular component: plasma membrane (traceable author statement from MGI).
GO:0016049;	Biological process: cell growth (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
IPR000886; ER_targeting_sequence.
IPR006620; Pro_4_hyd_alph.
IPR013026; TPR_region.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

SMART

SM00702; P4Hc; 1.
SMART graphical view of domain structure.

PROSITE

PS00014; ER_TARGET; 1.
PS50005; TPR; FALSE_NEG.
PS50293; TPR_REGION; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q3V1T4.

Genome annotation databases

Ensembl

ENSMUSG00000028641; Mus musculus. [Contig view]

GeneID

56401; -.

KEGG

mmu:56401; -.

Phylogenomic databases

HOVERGEN

Q3V1T4; -.

Other

SOURCE

Lepre1; Mus musculus.

ProtoNet

Q3V1T4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Coiled coil; Dioxygenase; Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Iron; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal; TPR repeat; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`	`Potential.`
`CHAIN`	`26 739`	`714`	`Prolyl 3-hydroxylase 1.`	`PRO_0000240353`
`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`	`404 442`	`39`	`Potential.`
`MOTIF`	`736 739`	`4`	`Prevents secretion from ER (Potential).`
`ACT_SITE`	`672 672`		`By similarity.`
`METAL`	`590 590`		`Iron.`
`METAL`	`592 592`		`Iron.`
`METAL`	`662 662`		`Iron.`
`CARBOHYD`	`319 319`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`470 470`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`543 543`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`1 179`		`Missing (in isoform 3).`	`VSP_019349`
`VAR_SEQ`	`540 543`		`MYYN -> TALQ (in isoform 2).`	`VSP_019350`
`VAR_SEQ`	`544 739`		`Missing (in isoform 2).`	`VSP_019351`
`CONFLICT`	`4 25`		`SERRLLAAMLAVAAAAALRVAA -> TKGGCWHDASGRRRRRLTGCG (in Ref. 1; AAF04806/AAF04807).`
`CONFLICT`	`50 50`		`G -> R (in Ref. 1; AAF04806/AAF04807).`
`CONFLICT`	`371 372`		`RS -> PN (in Ref. 1; AAF04806/AAF04807).`
`CONFLICT`	`403 403`		`P -> T (in Ref. 2; BAE21065).`
`CONFLICT`	`420 420`		`Missing (in Ref. 2; BAC26962).`
`CONFLICT`	`484 484`		`D -> N (in Ref. 2; BAE35138).`
`CONFLICT`	`569 569`		`L -> F (in Ref. 1; AAF04806).`
`CONFLICT`	`589 589`		`V -> D (in Ref. 2; BAE21065).`
`CONFLICT`	`601 601`		`L -> F (in Ref. 1; AAF04806).`
`CONFLICT`	`614 614`		`D -> E (in Ref. 1; AAF04806).`
`CONFLICT`	`685 685`		`H -> Q (in Ref. 2; BAC26962).`
`CONFLICT`	`716 716`		`D -> G (in Ref. 2; BAE35138 and 3; AAH24047).`
`CONFLICT`	`727 739`		`SLSDRGSLHKDEL -> FLHGATVLGVGIA (in Ref. 1; AAF04806).`

Sequence information

Length: 739 AA [This is the length of the unprocessed precursor]

Molecular weight: 83651 Da [This is the MW of the unprocessed precursor]

CRC64: 3484AE68E80B68E8 [This is a checksum on the sequence]

        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

Q3V1T4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools