F1LNN1 (F1LNN1_RAT) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Proteasome subunit beta type RuleBase RU004203
EC=3.4.25.1 RuleBase RU004203

Gene names

Name:

Psmb3 Ensembl ENSRNOP00000017377 RGD 61875

Organism

Rattus norvegicus (Rat) [Reference proteome] Ensembl ENSRNOP00000017377

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity By similarity. RuleBase RU004203
Catalytic activity	Cleavage of peptide bonds with very broad specificity. RuleBase RU000694
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits By similarity. RuleBase RU004203
Subcellular location	Cytoplasm. Nucleus By similarity RuleBase RU000694.
Sequence similarities	Belongs to the peptidase T1B family.
Caution	The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSRNOP00000017377

Ontologies

Keywords
Cellular component	Nucleus SAAS SAAS016050 Proteasome RuleBase RU000694
Molecular function	Hydrolase Protease Threonine protease RuleBase RU000694
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis involved in cellular protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	F1LNN1 [UniParc]. Last modified April 3, 2013. Version 2. Checksum: 4AFB18442D3F36DC	FASTA	205	22,978
	10 20 30 40 50 60 MSVMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV 70 80 90 100 110 120 QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF 130 140 150 160 170 180 ICSLDLIGCP MVTDDFVVSG TCSEQMYGMC ESLWEPNMEP EHLFETISTP MLNAVDRDAV 190 200 SGMGVIVHII EKDKITTRTL KARMD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Rat Genome Sequencing Project Consortium Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway Ensembl ENSRNOP00000017377.
[2]	Ensembl Submitted (JUL-2011) to UniProtKB Cited for: IDENTIFICATION. Strain: Brown Norway Ensembl ENSRNOP00000017377.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR06065478 Genomic DNA. No translation available.
IPI	IPI00214889.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000017377; ENSRNOP00000017377; ENSRNOG00000012938.
Organism-specific databases
RGD	61875. Psmb3.
Phylogenomic databases
GeneTree	ENSGT00550000074820.
Gene expression databases
ArrayExpress	F1LNN1.
Family and domain databases
InterPro	IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35575862.

Entry information

Entry name

F1LNN1_RAT

Accession

Primary (citable) accession number: F1LNN1

Entry history

Integrated into UniProtKB/TrEMBL:	May 3, 2011
Last sequence update:	April 3, 2013
Last modified:	May 1, 2013
This is version 15 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)