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P19324

- SERPH_MOUSE

UniProt

P19324 - SERPH_MOUSE

Protein

Serpin H1

Gene

Serpinh1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei376 – 3772Reactive bond homologBy similarity

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. serine-type endopeptidase inhibitor activity Source: RefGenome
    3. unfolded protein binding Source: MGI

    GO - Biological processi

    1. chondrocyte development involved in endochondral bone morphogenesis Source: MGI
    2. collagen biosynthetic process Source: MGI
    3. collagen fibril organization Source: MGI
    4. negative regulation of endopeptidase activity Source: RefGenome
    5. protein maturation Source: MGI
    6. regulation of proteolysis Source: RefGenome
    7. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

    Protein family/group databases

    MEROPSiI04.035.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serpin H1
    Alternative name(s):
    47 kDa heat shock protein
    Collagen-binding protein
    Short name:
    Colligin
    Serine protease inhibitor J6
    Gene namesi
    Name:Serpinh1
    Synonyms:Cbp1, Hsp47
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:88283. Serpinh1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    4. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    5. extracellular space Source: InterPro

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 417400Serpin H1PRO_0000032517Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei93 – 931N6-succinyllysine1 Publication
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
    Modified residuei206 – 2061N6-acetyllysine1 Publication
    Modified residuei295 – 2951N6-succinyllysine1 Publication
    Modified residuei318 – 3181N6-acetyllysine1 Publication
    Glycosylationi394 – 3941N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiP19324.
    PaxDbiP19324.
    PRIDEiP19324.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00114733.

    PTM databases

    PhosphoSiteiP19324.

    Expressioni

    Inductioni

    By heat shock and retinoic acid.

    Gene expression databases

    BgeeiP19324.
    GenevestigatoriP19324.

    Interactioni

    Protein-protein interaction databases

    BioGridi198530. 4 interactions.
    IntActiP19324. 1 interaction.
    MINTiMINT-1853582.

    Structurei

    3D structure databases

    ProteinModelPortaliP19324.
    SMRiP19324. Positions 35-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi414 – 4174Prevents secretion from ERCurated

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4826.
    GeneTreeiENSGT00750000117718.
    HOGENOMiHOG000238519.
    HOVERGENiHBG104930.
    InParanoidiQ5U4D0.
    KOiK09501.
    OMAiGVPMMHR.
    OrthoDBiEOG7GBFX4.
    TreeFamiTF343094.

    Family and domain databases

    InterProiIPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view]
    PANTHERiPTHR11461. PTHR11461. 1 hit.
    PfamiPF00079. Serpin. 1 hit.
    [Graphical view]
    SMARTiSM00093. SERPIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF56574. SSF56574. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00284. SERPIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P19324-1 [UniParc]FASTAAdd to Basket

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    MRSLLLGTLC LLAVALAAEV KKPLEAAAPG TAEKLSSKAT TLAERSTGLA    50
    FSLYQAMAKD QAVENILLSP LVVASSLGLV SLGGKATTAS QAKAVLSAEK 100
    LRDEEVHTGL GELLRSLSNS TARNVTWKLG SRLYGPSSVS FADDFVRSSK 150
    QHYNCEHSKI NFRDKRSALQ SINEWASQTT DGKLPEVTKD VERTDGALLV 200
    NAMFFKPHWD EKFHHKMVDN RGFMVTRSYT VGVTMMHRTG LYNYYDDEKE 250
    KLQMVEMPLA HKLSSLIILM PHHVEPLERL EKLLTKEQLK AWMGKMQKKA 300
    VAISLPKGVV EVTHDLQKHL AGLGLTEAID KNKADLSRMS GKKDLYLASV 350
    FHATAFEWDT EGNPFDQDIY GREELRSPKL FYADHPFIFL VRDNQSGSLL 400
    FIGRLVRPKG DKMRDEL 417
    Length:417
    Mass (Da):46,534
    Last modified:July 27, 2011 - v3
    Checksum:i1124A050A6CC4F67
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761A → P in AAA03200. (PubMed:2394749)Curated
    Sequence conflicti212 – 2121K → R in CAA43091. (PubMed:1317794)Curated
    Sequence conflicti212 – 2121K → R in AAA03200. (PubMed:2394749)Curated
    Sequence conflicti216 – 2161K → R in CAA43091. (PubMed:1317794)Curated
    Sequence conflicti216 – 2161K → R in AAA03200. (PubMed:2394749)Curated
    Sequence conflicti270 – 2712MP → IA in AAA03200. (PubMed:2394749)Curated
    Sequence conflicti277 – 2771L → S in AAA03200. (PubMed:2394749)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60676 mRNA. Translation: CAA43091.1.
    J05609 mRNA. Translation: AAA03200.1. Sequence problems.
    D12907 Genomic DNA. Translation: BAA02298.1.
    AK029080 mRNA. Translation: BAC26283.1.
    AK031457 mRNA. Translation: BAC27413.1.
    AK077660 mRNA. Translation: BAC36935.1.
    AK077937 mRNA. Translation: BAC37075.1.
    AK086519 mRNA. Translation: BAC39683.1.
    AK086523 mRNA. Translation: BAC39684.1.
    AK089993 mRNA. Translation: BAC41032.1.
    AK090103 mRNA. Translation: BAC41093.1.
    AK159998 mRNA. Translation: BAE35546.1.
    AK168442 mRNA. Translation: BAE40347.1.
    AK168870 mRNA. Translation: BAE40689.1.
    AC158748 Genomic DNA. No translation available.
    BC085143 mRNA. Translation: AAH85143.1.
    CCDSiCCDS21480.1.
    PIRiS23453. A42843.
    RefSeqiNP_001104513.1. NM_001111043.1.
    NP_001104514.1. NM_001111044.1.
    NP_001272705.1. NM_001285776.1.
    NP_033955.2. NM_009825.2.
    XP_006507341.1. XM_006507278.1.
    XP_006507342.1. XM_006507279.1.
    UniGeneiMm.22708.

    Genome annotation databases

    EnsembliENSMUST00000094154; ENSMUSP00000091706; ENSMUSG00000070436.
    ENSMUST00000169437; ENSMUSP00000126390; ENSMUSG00000070436.
    GeneIDi12406.
    KEGGimmu:12406.
    UCSCiuc009ilj.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60676 mRNA. Translation: CAA43091.1 .
    J05609 mRNA. Translation: AAA03200.1 . Sequence problems.
    D12907 Genomic DNA. Translation: BAA02298.1 .
    AK029080 mRNA. Translation: BAC26283.1 .
    AK031457 mRNA. Translation: BAC27413.1 .
    AK077660 mRNA. Translation: BAC36935.1 .
    AK077937 mRNA. Translation: BAC37075.1 .
    AK086519 mRNA. Translation: BAC39683.1 .
    AK086523 mRNA. Translation: BAC39684.1 .
    AK089993 mRNA. Translation: BAC41032.1 .
    AK090103 mRNA. Translation: BAC41093.1 .
    AK159998 mRNA. Translation: BAE35546.1 .
    AK168442 mRNA. Translation: BAE40347.1 .
    AK168870 mRNA. Translation: BAE40689.1 .
    AC158748 Genomic DNA. No translation available.
    BC085143 mRNA. Translation: AAH85143.1 .
    CCDSi CCDS21480.1.
    PIRi S23453. A42843.
    RefSeqi NP_001104513.1. NM_001111043.1.
    NP_001104514.1. NM_001111044.1.
    NP_001272705.1. NM_001285776.1.
    NP_033955.2. NM_009825.2.
    XP_006507341.1. XM_006507278.1.
    XP_006507342.1. XM_006507279.1.
    UniGenei Mm.22708.

    3D structure databases

    ProteinModelPortali P19324.
    SMRi P19324. Positions 35-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198530. 4 interactions.
    IntActi P19324. 1 interaction.
    MINTi MINT-1853582.

    Chemistry

    BindingDBi P19324.
    ChEMBLi CHEMBL1163113.

    Protein family/group databases

    MEROPSi I04.035.

    PTM databases

    PhosphoSitei P19324.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00114733.

    Proteomic databases

    MaxQBi P19324.
    PaxDbi P19324.
    PRIDEi P19324.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000094154 ; ENSMUSP00000091706 ; ENSMUSG00000070436 .
    ENSMUST00000169437 ; ENSMUSP00000126390 ; ENSMUSG00000070436 .
    GeneIDi 12406.
    KEGGi mmu:12406.
    UCSCi uc009ilj.2. mouse.

    Organism-specific databases

    CTDi 871.
    MGIi MGI:88283. Serpinh1.

    Phylogenomic databases

    eggNOGi COG4826.
    GeneTreei ENSGT00750000117718.
    HOGENOMi HOG000238519.
    HOVERGENi HBG104930.
    InParanoidi Q5U4D0.
    KOi K09501.
    OMAi GVPMMHR.
    OrthoDBi EOG7GBFX4.
    TreeFami TF343094.

    Enzyme and pathway databases

    Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    ChiTaRSi SERPINH1. mouse.
    NextBioi 281182.
    PROi P19324.
    SOURCEi Search...

    Gene expression databases

    Bgeei P19324.
    Genevestigatori P19324.

    Family and domain databases

    InterProi IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00284. SERPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells."
      Takechi H., Hirayoshi K., Nakai A., Kudo H., Saga S., Kita T., Nagata K.
      Eur. J. Biochem. 206:323-329(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-43.
      Strain: BALB/c.
    2. "A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue."
      Wang S.-Y., Gudas L.J.
      J. Biol. Chem. 265:15818-15822(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Teratocarcinoma.
    3. Erratum
      Wang S.-Y., Gudas L.J.
      J. Biol. Chem. 266:14135-14135(1991) [PubMed] [Europe PMC] [Abstract]
    4. "Structure of the gene and its retinoic acid-regulatory region for murine J6 serpin. An F9 teratocarcinoma cell retinoic acid-inducible protein."
      Wang S.-Y.
      J. Biol. Chem. 267:15362-15366(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Structure of the gene encoding the mouse 47-kDa heat-shock protein (HSP47)."
      Hosokawa N., Takechi H., Yokota S.I., Hirayoshi K., Nagata K.
      Gene 126:187-193(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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].
      Strain: C57BL/6J.
      Tissue: Head, Heart, Skin, Stomach and Testis.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    8. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-318, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-93 AND LYS-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSERPH_MOUSE
    AccessioniPrimary (citable) accession number: P19324
    Secondary accession number(s): Q5U4D0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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