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Protein
Submitted name:

Uncharacterized protein

Gene

SERPINH1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei315 – 3151SuccinateCombined sources

GO - Molecular functioni

  1. collagen binding Source: GO_Central
  2. poly(A) RNA binding Source: Ensembl
  3. serine-type endopeptidase inhibitor activity Source: GO_Central

GO - Biological processi

  1. chondrocyte development involved in endochondral bone morphogenesis Source: Ensembl
  2. collagen biosynthetic process Source: Ensembl
  3. collagen fibril organization Source: GO_Central
  4. negative regulation of endopeptidase activity Source: GO_Central
  5. protein maturation Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_279832. Collagen biosynthesis and modifying enzymes.

Names & Taxonomyi

Protein namesi
Submitted name:
Uncharacterized proteinImported
Gene namesi
Name:SERPINH1Imported
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)Imported
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Chromosome 21

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
  2. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZHAX-ray2.55A/B/C/D/K/L/P/Q36-418[»]
4AU3X-ray2.78A/B/C/D36-418[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 664Succinate bindingCombined sources

Sequence similaritiesi

Belongs to the serpin family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00770000120524.
InParanoidiE2RHY7.
KOiK09501.
OMAiNYEHSKI.
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.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E2RHY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFLLLLNTC CLLAVVLAAE VKKPAAAAAP GSAEKLSPKA ATLAERSAGL
60 70 80 90 100
AFSLYQAMAK DQAVENILLS PVVVASSLGL VSLGGKATTA SQAKAVLSAE
110 120 130 140 150
QLRDEEVHAG LGELLRSLSN STARNVTWKL GSRLYGPSSV SFAEDFVRSS
160 170 180 190 200
KQHYNCEHSK INFRDKRSAL QSINEWAAQT TDGKLPEVTK DVERTDGALL
210 220 230 240 250
VNAMFFKPHW DEKFHHKMVD NRGFMVTRSY TVGVTMMHRT GLYNYYDDEK
260 270 280 290 300
EKLQIVEMPL AHKLSSLIIL MPHHVEPLER LEKLLTKEQL KIWMGKMQKK
310 320 330 340 350
AVAISLPKGV VEVTHDLQKH LAGLGLTEAI DKNKADLSRM SGKKDLYLAS
360 370 380 390 400
VFHATAFEWD TEGNPFDQDI YGREELRSPK LFYADHPFIF LVRDTQSGSL
410
LFIGRLVRPK GDKMRDEL
Length:418
Mass (Da):46,583
Last modified:November 30, 2010 - v1
Checksum:iC15CF571FF20D3A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03012798 Genomic DNA. No translation available.
AAEX03012799 Genomic DNA. No translation available.
RefSeqiNP_001159360.1. NM_001165888.1.
XP_005633353.1. XM_005633296.1.
UniGeneiCfa.6125.

Genome annotation databases

EnsembliENSCAFT00000008665; ENSCAFP00000008031; ENSCAFG00000005386.
GeneIDi485187.
KEGGicfa:485187.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03012798 Genomic DNA. No translation available.
AAEX03012799 Genomic DNA. No translation available.
RefSeqiNP_001159360.1. NM_001165888.1.
XP_005633353.1. XM_005633296.1.
UniGeneiCfa.6125.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZHAX-ray2.55A/B/C/D/K/L/P/Q36-418[»]
4AU3X-ray2.78A/B/C/D36-418[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000008665; ENSCAFP00000008031; ENSCAFG00000005386.
GeneIDi485187.
KEGGicfa:485187.

Organism-specific databases

CTDi871.

Phylogenomic databases

GeneTreeiENSGT00770000120524.
InParanoidiE2RHY7.
KOiK09501.
OMAiNYEHSKI.
OrthoDBiEOG7GBFX4.
TreeFamiTF343094.

Enzyme and pathway databases

ReactomeiREACT_279832. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

NextBioi20859226.

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.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Broad Sequencing Platform
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BoxerImported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: BoxerImported.
  3. "Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition."
    Widmer C., Gebauer J.M., Brunstein E., Rosenbaum S., Zaucke F., Drogemuller C., Leeb T., Baumann U.
    Proc. Natl. Acad. Sci. U.S.A. 109:13243-13247(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 36-418 IN COMPLEX WITH SUCCINATE.

Entry informationi

Entry nameiE2RHY7_CANFA
AccessioniPrimary (citable) accession number: E2RHY7
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: April 1, 2015
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.