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Q6IE14 (TM11L_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transmembrane protease serine 11B-like protein

EC=3.4.21.-
Alternative name(s):
Airway trypsin-like protease 5
Transmembrane protease serine 11B
Gene names
Name:Tmprss11bnl
Synonyms:Hatl5, Tmprss11b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable serine protease By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein Potential.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 1 SEA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Transmembrane protease serine 11B-like protein
PRO_0000299321

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 4021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain41 – 420380Extracellular Potential
Domain48 – 165118SEA
Domain189 – 419231Peptidase S1

Sites

Active site2291Charge relay system By similarity
Active site2741Charge relay system By similarity
Active site3701Charge relay system By similarity

Amino acid modifications

Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Disulfide bond214 ↔ 230 By similarity
Disulfide bond339 ↔ 355 By similarity
Disulfide bond366 ↔ 395 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6IE14 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BC0D61CB9761AD2F

FASTA42047,242
        10         20         30         40         50         60 
MTVSKLRPVI ASRKSFPPWM IILGVLGVLA ILGLIIGLLV HFLAVENKIY YYQGSFKVLN 

        70         80         90        100        110        120 
IPYDRNYERE TSLESNYLSK ILEIKMVDAF ESSNIYKQYI NSQIITLVPE NNSVTAHIWL 

       130        140        150        160        170        180 
VFKDPWSNKE NLRRRIESIL HQMLENNSGS LTTDPGSLKL TEITKVDAEK IINNRCGRRP 

       190        200        210        220        230        240 
RMSATYDRIT GGSTAQKGEW PWQASLRVNG KHHCGASLIG ERFLLTAAHC FLRTNNPKNL 

       250        260        270        280        290        300 
TVSFGTRVTP AYMQHYVEEV IIHEDYVKGQ HHDDVAIIKL TEKVSFRNDV HRVCLPEATQ 

       310        320        330        340        350        360 
VFPPGEGVVV TGWGSLSYNG KSPLLLQKAS IKIIDTNACN SEEAYGGRIM DTMLCAGYME 

       370        380        390        400        410        420 
GYVDACQGDS GGPLVHPNSR DIWYLVGIVS WGHECGRVNK PGVYMRVTSY RDWIASKTGI 

« Hide

References

« Hide '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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03092659 Genomic DNA. No translation available.
AABR03092237 Genomic DNA. No translation available.
BN000379 mRNA. Translation: CAE51905.1.
RefSeqNP_001004020.1. NM_001004020.1.
UniGeneRn.138998.

3D structure databases

ProteinModelPortalQ6IE14.
SMRQ6IE14. Positions 189-420.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.207.

Proteomic databases

PRIDEQ6IE14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002743; ENSRNOP00000002743; ENSRNOG00000002002.
GeneID365265.
KEGGrno:365265.
UCSCRGD:1303278. rat.

Organism-specific databases

CTD132724.
RGD1303278. Tmprss11bnl.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00720000108393.
HOGENOMHOG000251823.
HOVERGENHBG013304.
InParanoidQ6IE14.
KOK09751.
OMAIINNRCG.
OrthoDBEOG75B84T.
PhylomeDBQ6IE14.
TreeFamTF351684.

Gene expression databases

GenevestigatorQ6IE14.

Family and domain databases

Gene3D3.30.70.960. 1 hit.
InterProIPR017329. Pept_S1A_HAT/DESC1.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF037941. TMPRSS11ABCDE. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF82671. SSF82671. 1 hit.
PROSITEPS50024. SEA. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio687004.
PROQ6IE14.

Entry information

Entry nameTM11L_RAT
AccessionPrimary (citable) accession number: Q6IE14
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries