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P19324 (SERPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serpin H1
Alternative name(s):
47 kDa heat shock protein
Collagen-binding protein
Short name=Colligin
Serine protease inhibitor J6
Gene names
Name:Serpinh1
Synonyms:Cbp1, Hsp47
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Endoplasmic reticulum lumen.

Induction

By heat shock and retinoic acid.

Sequence similarities

Belongs to the serpin family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionChaperone
   PTMAcetylation
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchondrocyte development involved in endochondral bone morphogenesis

Inferred from mutant phenotype PubMed 22492985. Source: MGI

collagen biosynthetic process

Inferred from mutant phenotype PubMed 10995453. Source: MGI

collagen fibril organization

Inferred from mutant phenotype PubMed 10995453PubMed 22492985. Source: MGI

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein maturation

Inferred from mutant phenotype PubMed 10995453. Source: MGI

regulation of proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 8018053. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 21606205. Source: MGI

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 10862616. Source: MGI

serine-type endopeptidase inhibitor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

unfolded protein binding

Inferred from direct assay PubMed 10862616. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.1
Chain18 – 417400Serpin H1
PRO_0000032517

Regions

Motif414 – 4174Prevents secretion from ER Probable

Sites

Site376 – 3772Reactive bond homolog By similarity

Amino acid modifications

Modified residue931N6-succinyllysine Ref.9
Modified residue2061N6-acetyllysine Ref.9
Modified residue2951N6-succinyllysine Ref.9
Modified residue3181N6-acetyllysine Ref.9
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1761A → P in AAA03200. Ref.2
Sequence conflict2121K → R in CAA43091. Ref.1
Sequence conflict2121K → R in AAA03200. Ref.2
Sequence conflict2161K → R in CAA43091. Ref.1
Sequence conflict2161K → R in AAA03200. Ref.2
Sequence conflict270 – 2712MP → IA in AAA03200. Ref.2
Sequence conflict2771L → S in AAA03200. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19324 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 1124A050A6CC4F67

FASTA41746,534
        10         20         30         40         50         60 
MRSLLLGTLC LLAVALAAEV KKPLEAAAPG TAEKLSSKAT TLAERSTGLA FSLYQAMAKD 

        70         80         90        100        110        120 
QAVENILLSP LVVASSLGLV SLGGKATTAS QAKAVLSAEK LRDEEVHTGL GELLRSLSNS 

       130        140        150        160        170        180 
TARNVTWKLG SRLYGPSSVS FADDFVRSSK QHYNCEHSKI NFRDKRSALQ SINEWASQTT 

       190        200        210        220        230        240 
DGKLPEVTKD VERTDGALLV NAMFFKPHWD EKFHHKMVDN RGFMVTRSYT VGVTMMHRTG 

       250        260        270        280        290        300 
LYNYYDDEKE KLQMVEMPLA HKLSSLIILM PHHVEPLERL EKLLTKEQLK AWMGKMQKKA 

       310        320        330        340        350        360 
VAISLPKGVV EVTHDLQKHL AGLGLTEAID KNKADLSRMS GKKDLYLASV FHATAFEWDT 

       370        380        390        400        410 
EGNPFDQDIY GREELRSPKL FYADHPFIFL VRDNQSGSLL FIGRLVRPKG DKMRDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS21480.1.
PIRA42843. S23453.
RefSeqNP_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.
UniGeneMm.22708.

3D structure databases

ProteinModelPortalP19324.
SMRP19324. Positions 35-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198530. 4 interactions.
IntActP19324. 1 interaction.
MINTMINT-1853582.

Chemistry

BindingDBP19324.
ChEMBLCHEMBL1163113.

Protein family/group databases

MEROPSI04.035.

PTM databases

PhosphoSiteP19324.

2D gel databases

REPRODUCTION-2DPAGEIPI00114733.

Proteomic databases

MaxQBP19324.
PaxDbP19324.
PRIDEP19324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000094154; ENSMUSP00000091706; ENSMUSG00000070436.
ENSMUST00000169437; ENSMUSP00000126390; ENSMUSG00000070436.
GeneID12406.
KEGGmmu:12406.
UCSCuc009ilj.2. mouse.

Organism-specific databases

CTD871.
MGIMGI:88283. Serpinh1.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00750000117718.
HOGENOMHOG000238519.
HOVERGENHBG104930.
InParanoidQ5U4D0.
KOK09501.
OMAGVPMMHR.
OrthoDBEOG7GBFX4.
TreeFamTF343094.

Gene expression databases

BgeeP19324.
GenevestigatorP19324.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSERPINH1. mouse.
NextBio281182.
PROP19324.
SOURCESearch...

Entry information

Entry nameSERPH_MOUSE
AccessionPrimary (citable) accession number: P19324
Secondary accession number(s): Q5U4D0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot