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Protein

Cystatin-C

Gene

Cst3

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

Functioni

As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei31 – 311Reactive site

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Protein family/group databases

MEROPSiI25.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystatin-C
Alternative name(s):
Cystatin-3
Gene namesi
Name:Cst3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:102519. Cst3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 140120Cystatin-CPRO_0000006642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi93 ↔ 103By similarity
Disulfide bondi117 ↔ 137By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP21460.
MaxQBiP21460.
PaxDbiP21460.
PRIDEiP21460.

PTM databases

iPTMnetiP21460.
PhosphoSiteiP21460.

Expressioni

Gene expression databases

BgeeiP21460.
CleanExiMM_CST3.
ExpressionAtlasiP21460. baseline and differential.
GenevisibleiP21460. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP21460. 3 interactions.
MINTiMINT-4092770.
STRINGi10090.ENSMUSP00000028938.

Structurei

3D structure databases

ProteinModelPortaliP21460.
SMRiP21460. Positions 31-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi75 – 795Secondary area of contact

Sequence similaritiesi

Belongs to the cystatin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IZZH. Eukaryota.
ENOG4112CFJ. LUCA.
GeneTreeiENSGT00840000129787.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP21460.
KOiK13899.
OMAiYTVPWLG.
OrthoDBiEOG7M98J9.
PhylomeDBiP21460.

Family and domain databases

InterProiIPR027214. Cystatin.
IPR000010. Cystatin_dom.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PANTHERiPTHR11413. PTHR11413. 1 hit.
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 1 hit.
[Graphical view]
PROSITEiPS00287. CYSTATIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21460-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPLRSLLF LLAVLAVAWA ATPKQGPRML GAPEEADANE EGVRRALDFA
60 70 80 90 100
VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL
110 120 130 140
TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA
Length:140
Mass (Da):15,531
Last modified:February 1, 1996 - v2
Checksum:i3A563406DD58D0F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → G in AAA63298 (PubMed:2241983).Curated
Sequence conflicti84 – 841L → F in AAA63298 (PubMed:2241983).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59470 mRNA. Translation: AAA63298.1.
U10098 Unassigned DNA. Translation: AAB41056.1.
AF483486 mRNA. Translation: AAL90760.1.
AF483487 mRNA. Translation: AAL90761.1.
AK002438 mRNA. Translation: BAB22101.1.
AK013676 mRNA. Translation: BAB28949.1.
AK014368 mRNA. Translation: BAB29303.1.
AK131728 mRNA. Translation: BAE20785.1.
AK146333 mRNA. Translation: BAE27088.1.
AK151160 mRNA. Translation: BAE30165.1.
AK161856 mRNA. Translation: BAE36608.1.
AK166430 mRNA. Translation: BAE38771.1.
BC002072 mRNA. Translation: AAH02072.1.
CCDSiCCDS16852.1.
PIRiA36163.
RefSeqiNP_034106.2. NM_009976.4.
UniGeneiMm.4263.

Genome annotation databases

EnsembliENSMUST00000028938; ENSMUSP00000028938; ENSMUSG00000027447.
GeneIDi13010.
KEGGimmu:13010.
UCSCiuc008mtt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59470 mRNA. Translation: AAA63298.1.
U10098 Unassigned DNA. Translation: AAB41056.1.
AF483486 mRNA. Translation: AAL90760.1.
AF483487 mRNA. Translation: AAL90761.1.
AK002438 mRNA. Translation: BAB22101.1.
AK013676 mRNA. Translation: BAB28949.1.
AK014368 mRNA. Translation: BAB29303.1.
AK131728 mRNA. Translation: BAE20785.1.
AK146333 mRNA. Translation: BAE27088.1.
AK151160 mRNA. Translation: BAE30165.1.
AK161856 mRNA. Translation: BAE36608.1.
AK166430 mRNA. Translation: BAE38771.1.
BC002072 mRNA. Translation: AAH02072.1.
CCDSiCCDS16852.1.
PIRiA36163.
RefSeqiNP_034106.2. NM_009976.4.
UniGeneiMm.4263.

3D structure databases

ProteinModelPortaliP21460.
SMRiP21460. Positions 31-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21460. 3 interactions.
MINTiMINT-4092770.
STRINGi10090.ENSMUSP00000028938.

Protein family/group databases

MEROPSiI25.004.

PTM databases

iPTMnetiP21460.
PhosphoSiteiP21460.

Proteomic databases

EPDiP21460.
MaxQBiP21460.
PaxDbiP21460.
PRIDEiP21460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028938; ENSMUSP00000028938; ENSMUSG00000027447.
GeneIDi13010.
KEGGimmu:13010.
UCSCiuc008mtt.1. mouse.

Organism-specific databases

CTDi1471.
MGIiMGI:102519. Cst3.

Phylogenomic databases

eggNOGiENOG410IZZH. Eukaryota.
ENOG4112CFJ. LUCA.
GeneTreeiENSGT00840000129787.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP21460.
KOiK13899.
OMAiYTVPWLG.
OrthoDBiEOG7M98J9.
PhylomeDBiP21460.

Miscellaneous databases

PROiP21460.
SOURCEiSearch...

Gene expression databases

BgeeiP21460.
CleanExiMM_CST3.
ExpressionAtlasiP21460. baseline and differential.
GenevisibleiP21460. MM.

Family and domain databases

InterProiIPR027214. Cystatin.
IPR000010. Cystatin_dom.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PANTHERiPTHR11413. PTHR11413. 1 hit.
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 1 hit.
[Graphical view]
PROSITEiPS00287. CYSTATIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transforming growth factor beta regulates cystatin C in serum-free mouse embryo (SFME) cells."
    Solem M., Rawson C., Lindburg K., Barnes D.
    Biochem. Biophys. Res. Commun. 172:945-951(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Structural organization, expression and chromosomal mapping of the mouse cystatin-C-encoding gene (Cst3)."
    Huh C., Nagle J.W., Kozak C.A., Abrahamson M., Karlsson S.
    Gene 152:221-226(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
    Tissue: Liver.
  3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ILS and ISS.
  4. "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 and DBA/2.
    Tissue: Bone marrow, Head, Hippocampus, Kidney, Mammary gland, Medulla oblongata and Testis.
  5. "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].
  6. 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 nameiCYTC_MOUSE
AccessioniPrimary (citable) accession number: P21460
Secondary accession number(s): Q544Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 148 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

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.