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Q3V1T4

- P3H1_MOUSE

UniProt

Q3V1T4 - P3H1_MOUSE

Protein

Prolyl 3-hydroxylase 1

Gene

Lepre1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (27 Jun 2006)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-3-hydroxy-L-proline-[procollagen] + succinate + CO2.

    Cofactori

    Iron.By similarity
    Ascorbate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi590 – 5901Iron
    Metal bindingi592 – 5921Iron
    Metal bindingi662 – 6621Iron
    Active sitei672 – 6721By similarity

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. L-ascorbic acid binding Source: UniProtKB-KW
    3. procollagen-proline 3-dioxygenase activity Source: MGI

    GO - Biological processi

    1. cell growth Source: MGI
    2. collagen fibril organization Source: MGI
    3. collagen metabolic process Source: MGI
    4. peptidyl-proline hydroxylation Source: GOC
    5. regulation of ossification Source: MGI

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl 3-hydroxylase 1 (EC:1.14.11.7)
    Alternative name(s):
    Growth suppressor 1
    Leucine- and proline-enriched proteoglycan 1
    Short name:
    Leprecan-1
    Gene namesi
    Name:Lepre1
    Synonyms:Gros1, P3h1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1888921. Lepre1.

    Subcellular locationi

    Endoplasmic reticulum PROSITE-ProRule annotation. Secretedextracellular spaceextracellular matrix By similarity
    Note: Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG).

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. nucleus Source: MGI
    4. plasma membrane Source: MGI
    5. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 739714Prolyl 3-hydroxylase 1PRO_0000240353Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    O-glycosylated; chondroitin sulfate.By similarity

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ3V1T4.
    PRIDEiQ3V1T4.

    PTM databases

    PhosphoSiteiQ3V1T4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ3V1T4.
    BgeeiQ3V1T4.
    CleanExiMM_LEPRE1.
    GenevestigatoriQ3V1T4.

    Interactioni

    Protein-protein interaction databases

    IntActiQ3V1T4. 1 interaction.
    MINTiMINT-4125499.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3V1T4.
    SMRiQ3V1T4. Positions 34-65.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati36 – 6934TPR 1Add
    BLAST
    Repeati146 – 17934TPR 2Add
    BLAST
    Repeati208 – 24134TPR 3Add
    BLAST
    Repeati304 – 33734TPR 4Add
    BLAST
    Domaini567 – 681115Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili404 – 44239Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi736 – 7394Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the leprecan family.Curated
    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
    Contains 4 TPR repeats.Curated

    Keywords - Domaini

    Coiled coil, Repeat, Signal, TPR repeat

    Phylogenomic databases

    eggNOGiNOG269251.
    GeneTreeiENSGT00550000074573.
    HOVERGENiHBG053224.
    KOiK08134.
    OrthoDBiEOG7BZVSS.

    Family and domain databases

    Gene3Di1.25.40.10. 3 hits.
    InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
    [Graphical view]
    SMARTiSM00702. P4Hc. 1 hit.
    [Graphical view]
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS51471. FE2OG_OXY. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3V1T4-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAVSERRLLA AMLAVAAAAA LRVAAESEPG WDVAAPDLLY AEGTAAYSRG    50
    DWPGVVLNME RALRSRAALR ALRLRCRTRC ATELPWAPDL DLGPDPSLSQ 100
    DPGAAALHDL RFFGAVLRRA ACLRRCLGPP SAHLLSEELD LEFNKRSPYN 150
    YLQVAYFKIN KLEKAVAAAH TFFVGNPEHM EMRQNLDYYQ TMSGVKEADF 200
    RDLEAKPHMH EFRLGVRLYS EEKPQEAVPH LEAALQEYFV ADEECRALCE 250
    GPYDYDGYNY LDYSADLFQA ITDHYVQVLN CKQNCVTELA SHPSREKPFE 300
    DFLPSHYNYL QFAYYNIGNY TQAIECAKTY LLFFPNDEVM HQNLAYYTAM 350
    LGEEEASSIS PRENAEEYRR RSLLEKELLF FAYDIFGIPF VDPDSWTPEE 400
    VIPKRLQEKQ KSERETAVRI SQEIGNLMKE IETLVEEKTK ESLDVSRLTR 450
    EGGPLLYEGI SLTMNSKVLN GSQRVVMDGV ISDDECQELQ RLTNAAATSG 500
    DGYRGQTSPH TPNEKFYGVT VLKALKLGQE GKVPLQSARM YYNVTEKVRR 550
    VMESYFRLDT PLYFSYSHLV CRTAIEESQA ERKDSSHPVH VDNCILNAEA 600
    LMCIKEPPAY TFRDYSAILY LNGDFDGGNF YFTELDAKTV TAEVQPQCGR 650
    AVGFSSGTEN PHGVKAVTRG QRCAIALWFT LDPRHSERDR VQADDLVKML 700
    FSPEEVDLPQ EQPLPDQQGS PEPGEESLSD RGSLHKDEL 739
    Length:739
    Mass (Da):83,651
    Last modified:June 27, 2006 - v2
    Checksum:i3484AE68E80B68E8
    GO
    Isoform 2 (identifier: Q3V1T4-2) [UniParc]FASTAAdd to Basket

    Also known as: GROS1-S

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

    Show »
    Length:543
    Mass (Da):61,397
    Checksum:i2166EB32EC38A766
    GO
    Isoform 3 (identifier: Q3V1T4-3) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:560
    Mass (Da):64,102
    Checksum:i673B7643F80A1388
    GO

    Sequence cautioni

    The sequence BAE21065.1 differs from that shown. Reason: Intron retention.
    The sequence BAB27041.1 differs from that shown. Reason: Frameshift at position 707.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 2522SERRL…LRVAA → TKGGCWHDASGRRRRRLTGC G in AAF04806. (PubMed:10951563)CuratedAdd
    BLAST
    Sequence conflicti4 – 2522SERRL…LRVAA → TKGGCWHDASGRRRRRLTGC G in AAF04807. (PubMed:10951563)CuratedAdd
    BLAST
    Sequence conflicti50 – 501G → R in AAF04806. (PubMed:10951563)Curated
    Sequence conflicti50 – 501G → R in AAF04807. (PubMed:10951563)Curated
    Sequence conflicti371 – 3722RS → PN in AAF04806. (PubMed:10951563)Curated
    Sequence conflicti371 – 3722RS → PN in AAF04807. (PubMed:10951563)Curated
    Sequence conflicti403 – 4031P → T in BAE21065. (PubMed:16141072)Curated
    Sequence conflicti420 – 4201Missing in BAC26962. (PubMed:16141072)Curated
    Sequence conflicti484 – 4841D → N in BAE35138. (PubMed:16141072)Curated
    Sequence conflicti569 – 5691L → F in AAF04806. (PubMed:10951563)Curated
    Sequence conflicti589 – 5891V → D in BAE21065. (PubMed:16141072)Curated
    Sequence conflicti601 – 6011L → F in AAF04806. (PubMed:10951563)Curated
    Sequence conflicti614 – 6141D → E in AAF04806. (PubMed:10951563)Curated
    Sequence conflicti685 – 6851H → Q in BAC26962. (PubMed:16141072)Curated
    Sequence conflicti716 – 7161D → G in BAE35138. (PubMed:16141072)Curated
    Sequence conflicti716 – 7161D → G in AAH24047. (PubMed:19468303)Curated
    Sequence conflicti727 – 73913SLSDR…HKDEL → FLHGATVLGVGIA in AAF04806. (PubMed:10951563)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 179179Missing in isoform 3. 1 PublicationVSP_019349Add
    BLAST
    Alternative sequencei540 – 5434MYYN → TALQ in isoform 2. 1 PublicationVSP_019350
    Alternative sequencei544 – 739196Missing in isoform 2. 1 PublicationVSP_019351Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    AL606975 Genomic DNA. Translation: CAM21645.1.
    AL606975 Genomic DNA. Translation: CAO78098.1.
    BC024047 mRNA. Translation: AAH24047.1.
    CCDSiCCDS38859.1. [Q3V1T4-1]
    CCDS38860.1. [Q3V1T4-3]
    RefSeqiNP_001035874.1. NM_001042411.1. [Q3V1T4-3]
    NP_001273077.1. NM_001286148.1.
    NP_062756.2. NM_019782.3.
    NP_062757.2. NM_019783.2. [Q3V1T4-1]
    UniGeneiMm.27961.

    Genome annotation databases

    EnsembliENSMUST00000081606; ENSMUSP00000080312; ENSMUSG00000028641. [Q3V1T4-3]
    ENSMUST00000121111; ENSMUSP00000112504; ENSMUSG00000028641. [Q3V1T4-1]
    GeneIDi56401.
    KEGGimmu:56401.
    UCSCiuc008ulq.1. mouse. [Q3V1T4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    AL606975 Genomic DNA. Translation: CAM21645.1 .
    AL606975 Genomic DNA. Translation: CAO78098.1 .
    BC024047 mRNA. Translation: AAH24047.1 .
    CCDSi CCDS38859.1. [Q3V1T4-1 ]
    CCDS38860.1. [Q3V1T4-3 ]
    RefSeqi NP_001035874.1. NM_001042411.1. [Q3V1T4-3 ]
    NP_001273077.1. NM_001286148.1.
    NP_062756.2. NM_019782.3.
    NP_062757.2. NM_019783.2. [Q3V1T4-1 ]
    UniGenei Mm.27961.

    3D structure databases

    ProteinModelPortali Q3V1T4.
    SMRi Q3V1T4. Positions 34-65.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q3V1T4. 1 interaction.
    MINTi MINT-4125499.

    PTM databases

    PhosphoSitei Q3V1T4.

    Proteomic databases

    PaxDbi Q3V1T4.
    PRIDEi Q3V1T4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081606 ; ENSMUSP00000080312 ; ENSMUSG00000028641 . [Q3V1T4-3 ]
    ENSMUST00000121111 ; ENSMUSP00000112504 ; ENSMUSG00000028641 . [Q3V1T4-1 ]
    GeneIDi 56401.
    KEGGi mmu:56401.
    UCSCi uc008ulq.1. mouse. [Q3V1T4-1 ]

    Organism-specific databases

    CTDi 64175.
    MGIi MGI:1888921. Lepre1.

    Phylogenomic databases

    eggNOGi NOG269251.
    GeneTreei ENSGT00550000074573.
    HOVERGENi HBG053224.
    KOi K08134.
    OrthoDBi EOG7BZVSS.

    Enzyme and pathway databases

    Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    NextBioi 312512.
    PROi Q3V1T4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3V1T4.
    Bgeei Q3V1T4.
    CleanExi MM_LEPRE1.
    Genevestigatori Q3V1T4.

    Family and domain databases

    Gene3Di 1.25.40.10. 3 hits.
    InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF13640. 2OG-FeII_Oxy_3. 1 hit.
    [Graphical view ]
    SMARTi SM00702. P4Hc. 1 hit.
    [Graphical view ]
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J.
      Tissue: Embryonic stem cell, Pituitary and Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiP3H1_MOUSE
    AccessioniPrimary (citable) accession number: Q3V1T4
    Secondary accession number(s): A2A7Q4
    , A6PW85, Q3TWX8, Q8BSV2, Q8CFL3, Q9CWK5, Q9QZT6, Q9QZT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: June 27, 2006
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3