Q6IE06 (PRS58_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative inactive serine protease 58
EC=3.4.21.4

Alternative name(s):
Trypsin-X3

Gene names

Name:	Prss58
Synonyms:	Tryx3

Organism

Rattus norvegicus (Rat) [Reference proteome]

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	240 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.
Caution	Thr-195 is present instead of the conserved Ser which is expected to be an active site residue. It is therefore unsure if this protein has kept its catalytic activity.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 240	224	Putative inactive serine protease 58		PRO_5000096013
Regions
	Domain	17 – 238	222	Peptidase S1
Sites
	Active site	55	1	Charge relay system By similarity
	Active site	100	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	155	1	N-linked (GlcNAc...) Potential
	Disulfide bond	40 ↔ 56		By similarity
	Disulfide bond	132 ↔ 200		By similarity
	Disulfide bond	164 ↔ 179		By similarity
	Disulfide bond	190 ↔ 214		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6IE06 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 0A7841D62039FB8A	FASTA	240	26,812
	10 20 30 40 50 60 MKLVFCILST LLGTFAYNPD HIAGTTPPYL VYLKSDYLPC TGVLIHPLWV VTSAHCNLPD 70 80 90 100 110 120 LRVILGITNP ADTTEHDVEV SDYEKMFRHP YFSVSSISYD LMLIKLRRGI KHSYYAKAVK 130 140 150 160 170 180 LPQHTVPVNA MCSVSTWAYN LCDVTKEPDS LQTVNVSVIS KAECHNAYKA FDIRENMICV 190 200 210 220 230 240 GIVPGRRLPC KEVTAAPAVC NGVLYGILSY ADGCVLRADV GIYASIFHYM PWIENIMKNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." 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.
[2]	"A genomic analysis of rat proteases and protease inhibitors." Puente X.S., Lopez-Otin C. Genome Res. 14:609-622(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION. Strain: Sprague-Dawley.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC094798 Genomic DNA. No translation available. BN000387 mRNA. Translation: CAE51913.1.
IPI	IPI00421739.
RefSeq	NP_001009174.1. NM_001009174.1.
UniGene	Rn.125929.
3D structure databases
HSSP	HSSP built from PDB template 1EPT based on UniProtKB P00761.
ProteinModelPortal	Q6IE06.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000017611.
Protein family/group databases
MEROPS	S01.984.
Proteomic databases
PRIDE	Q6IE06.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000017611; ENSRNOP00000017611; ENSRNOG00000013132.
GeneID	408204.
KEGG	rno:408204.
UCSC	RGD:1303054. rat.
Organism-specific databases
CTD	136541.
RGD	1303054. Prss58.
Phylogenomic databases
eggNOG	COG5640.
GeneTree	ENSGT00690000101952.
HOVERGEN	HBG013304.
InParanoid	Q6IE06.
OMA	VSTWAYN.
OrthoDB	EOG405S20.
Gene expression databases
Genevestigator	Q6IE06.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. False negative. PS00135. TRYPSIN_SER. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	696400.

Entry information

Entry name

PRS58_RAT

Accession

Primary (citable) accession number: Q6IE06

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program