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Protein

Retinoid-inducible serine carboxypeptidase

Gene

Scpep1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in vascular wall and kidney homeostasis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei167 – 1671PROSITE-ProRule annotation
Active sitei371 – 3711PROSITE-ProRule annotation
Active sitei431 – 4311PROSITE-ProRule annotation

GO - Molecular functioni

  • serine-type carboxypeptidase activity Source: UniProtKB

GO - Biological processi

  • negative regulation of blood pressure Source: UniProtKB
  • positive regulation of vasodilation Source: UniProtKB
  • retinoic acid metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.16.5. 3474.

Protein family/group databases

ESTHERimouse-RISC. Carboxypeptidase_S10.
MEROPSiS10.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoid-inducible serine carboxypeptidase (EC:3.4.16.-)
Alternative name(s):
Serine carboxypeptidase 1
Gene namesi
Name:Scpep1
Synonyms:Risc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1921867. Scpep1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3259511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 452424Retinoid-inducible serine carboxypeptidasePRO_0000004285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysis
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence analysis
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence analysis
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence analysis
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ920A5.
MaxQBiQ920A5.
PaxDbiQ920A5.
PRIDEiQ920A5.

PTM databases

iPTMnetiQ920A5.
PhosphoSiteiQ920A5.
SwissPalmiQ920A5.

Expressioni

Gene expression databases

BgeeiQ920A5.
CleanExiMM_SCPEP1.
GenevisibleiQ920A5. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000287.

Structurei

3D structure databases

ProteinModelPortaliQ920A5.
SMRiQ920A5. Positions 32-225, 308-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1283. Eukaryota.
COG2939. LUCA.
GeneTreeiENSGT00790000123063.
HOGENOMiHOG000242971.
HOVERGENiHBG002816.
InParanoidiQ920A5.
KOiK09646.
OMAiIILEQAN.
OrthoDBiEOG7DC245.
TreeFamiTF313740.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q920A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSRRICLV RLWLLLLSFL LGFSAGSAID WREPEGKEVW DYVTVRKDAH
60 70 80 90 100
MFWWLYYATN PCKNFSELPL VMWLQGGPGG SSTGFGNFEE IGPLDTQLKP
110 120 130 140 150
RNTTWLQWAS LLFVDNPVGT GFSYVNTTDA YAKDLDTVAS DMMVLLKSFF
160 170 180 190 200
DCHKEFQTVP FYIFSESYGG KMAAGISVEL YKAVQQGTIK CNFSGVALGD
210 220 230 240 250
SWISPVDSVL SWGPYLYSMS LLDNQGLAEV SDIAEQVLDA VNKGFYKEAT
260 270 280 290 300
QLWGKAEMII EKNTDGVNFY NILTKSSPEK AMESSLEFLR SPLVRLCQRH
310 320 330 340 350
VRHLQGDALS QLMNGPIKKK LKIIPEDISW GAQASYVFLS MEGDFMKPAI
360 370 380 390 400
DVVDKLLAAG VNVTVYNGQL DLIVDTIGQE SWVQKLKWPQ LSKFNQLKWK
410 420 430 440 450
ALYTDPKSSE TAAFVKSYEN LAFYWILKAG HMVPSDQGEM ALKMMKLVTK

QE
Length:452
Mass (Da):50,965
Last modified:July 27, 2011 - v2
Checksum:iE0E59F635B21B051
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291E → M in AAK84662 (PubMed:11447226).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF330052 mRNA. Translation: AAK84662.1.
AK014680 mRNA. Translation: BAB29501.1.
AK050181 mRNA. Translation: BAC34111.1.
AK153225 mRNA. Translation: BAE31818.1.
AL646096, AL929426 Genomic DNA. Translation: CAI24260.1.
AL929426, AL646096 Genomic DNA. Translation: CAI25809.1.
CCDSiCCDS25230.1.
RefSeqiNP_083299.3. NM_029023.3.
UniGeneiMm.34126.

Genome annotation databases

EnsembliENSMUST00000000287; ENSMUSP00000000287; ENSMUSG00000000278.
GeneIDi74617.
KEGGimmu:74617.
UCSCiuc007kvx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF330052 mRNA. Translation: AAK84662.1.
AK014680 mRNA. Translation: BAB29501.1.
AK050181 mRNA. Translation: BAC34111.1.
AK153225 mRNA. Translation: BAE31818.1.
AL646096, AL929426 Genomic DNA. Translation: CAI24260.1.
AL929426, AL646096 Genomic DNA. Translation: CAI25809.1.
CCDSiCCDS25230.1.
RefSeqiNP_083299.3. NM_029023.3.
UniGeneiMm.34126.

3D structure databases

ProteinModelPortaliQ920A5.
SMRiQ920A5. Positions 32-225, 308-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000287.

Chemistry

ChEMBLiCHEMBL3259511.

Protein family/group databases

ESTHERimouse-RISC. Carboxypeptidase_S10.
MEROPSiS10.013.

PTM databases

iPTMnetiQ920A5.
PhosphoSiteiQ920A5.
SwissPalmiQ920A5.

Proteomic databases

EPDiQ920A5.
MaxQBiQ920A5.
PaxDbiQ920A5.
PRIDEiQ920A5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000287; ENSMUSP00000000287; ENSMUSG00000000278.
GeneIDi74617.
KEGGimmu:74617.
UCSCiuc007kvx.2. mouse.

Organism-specific databases

CTDi59342.
MGIiMGI:1921867. Scpep1.

Phylogenomic databases

eggNOGiKOG1283. Eukaryota.
COG2939. LUCA.
GeneTreeiENSGT00790000123063.
HOGENOMiHOG000242971.
HOVERGENiHBG002816.
InParanoidiQ920A5.
KOiK09646.
OMAiIILEQAN.
OrthoDBiEOG7DC245.
TreeFamiTF313740.

Enzyme and pathway databases

BRENDAi3.4.16.5. 3474.

Miscellaneous databases

ChiTaRSiScpep1. mouse.
NextBioi341225.
PROiQ920A5.
SOURCEiSearch...

Gene expression databases

BgeeiQ920A5.
CleanExiMM_SCPEP1.
GenevisibleiQ920A5. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a novel retinoid-inducible serine carboxypeptidase from vascular smooth muscle cells."
    Chen J., Streb J.W., Maltby K.M., Kitchen C.M., Miano J.M.
    J. Biol. Chem. 276:34175-34181(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Head and Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRISC_MOUSE
AccessioniPrimary (citable) accession number: Q920A5
Secondary accession number(s): Q9D625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 112 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. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.