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Protein

Transmembrane protease serine 11B-like protein

Gene

Tmprss11bnl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Serine protease.By similarity

Enzyme regulationi

Inhibited by aprotinin, leupeptin, benzamidine, SERPINA1, SPINT1 and SPINT2.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei229 – 2291Charge relay systemBy similarity
Active sitei274 – 2741Charge relay systemBy similarity
Active sitei370 – 3701Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.321.

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane protease serine 11B-like protein (EC:3.4.21.-)
Alternative name(s):
Airway trypsin-like protease 5
Transmembrane protease serine 11B
Gene namesi
Name:Tmprss11bnl
Synonyms:Hatl5, Tmprss11b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi1303278. Tmprss11bnl.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini41 – 420380ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Transmembrane protease serine 11B-like proteinPRO_0000299321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi214 ↔ 230PROSITE-ProRule annotation
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi339 ↔ 355PROSITE-ProRule annotation
Disulfide bondi366 ↔ 395PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ6IE14.

Structurei

3D structure databases

ProteinModelPortaliQ6IE14.
SMRiQ6IE14. Positions 189-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 165118SEAPROSITE-ProRule annotationAdd
BLAST
Domaini189 – 419231Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SEA domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251823.
HOVERGENiHBG013304.
InParanoidiQ6IE14.
KOiK09751.
OMAiIINNRCG.
OrthoDBiEOG75B84T.
PhylomeDBiQ6IE14.
TreeFamiTF351684.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR017329. Pept_S1A_HAT/DESC1.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF037941. TMPRSS11ABCDE. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF82671. SSF82671. 1 hit.
PROSITEiPS50024. SEA. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6IE14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVSKLRPVI ASRKSFPPWM IILGVLGVLA ILGLIIGLLV HFLAVENKIY
60 70 80 90 100
YYQGSFKVLN IPYDRNYERE TSLESNYLSK ILEIKMVDAF ESSNIYKQYI
110 120 130 140 150
NSQIITLVPE NNSVTAHIWL VFKDPWSNKE NLRRRIESIL HQMLENNSGS
160 170 180 190 200
LTTDPGSLKL TEITKVDAEK IINNRCGRRP RMSATYDRIT GGSTAQKGEW
210 220 230 240 250
PWQASLRVNG KHHCGASLIG ERFLLTAAHC FLRTNNPKNL TVSFGTRVTP
260 270 280 290 300
AYMQHYVEEV IIHEDYVKGQ HHDDVAIIKL TEKVSFRNDV HRVCLPEATQ
310 320 330 340 350
VFPPGEGVVV TGWGSLSYNG KSPLLLQKAS IKIIDTNACN SEEAYGGRIM
360 370 380 390 400
DTMLCAGYME GYVDACQGDS GGPLVHPNSR DIWYLVGIVS WGHECGRVNK
410 420
PGVYMRVTSY RDWIASKTGI
Length:420
Mass (Da):47,242
Last modified:July 5, 2004 - v1
Checksum:iBC0D61CB9761AD2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03092659 Genomic DNA. No translation available.
AABR03092237 Genomic DNA. No translation available.
BN000379 mRNA. Translation: CAE51905.1.
RefSeqiNP_001004020.1. NM_001004020.1.
UniGeneiRn.138998.

Genome annotation databases

EnsembliENSRNOT00000002743; ENSRNOP00000002743; ENSRNOG00000002002.
GeneIDi365265.
KEGGirno:365265.
UCSCiRGD:1303278. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03092659 Genomic DNA. No translation available.
AABR03092237 Genomic DNA. No translation available.
BN000379 mRNA. Translation: CAE51905.1.
RefSeqiNP_001004020.1. NM_001004020.1.
UniGeneiRn.138998.

3D structure databases

ProteinModelPortaliQ6IE14.
SMRiQ6IE14. Positions 189-420.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.321.

Proteomic databases

PRIDEiQ6IE14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002743; ENSRNOP00000002743; ENSRNOG00000002002.
GeneIDi365265.
KEGGirno:365265.
UCSCiRGD:1303278. rat.

Organism-specific databases

CTDi132724.
RGDi1303278. Tmprss11bnl.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251823.
HOVERGENiHBG013304.
InParanoidiQ6IE14.
KOiK09751.
OMAiIINNRCG.
OrthoDBiEOG75B84T.
PhylomeDBiQ6IE14.
TreeFamiTF351684.

Miscellaneous databases

NextBioi687004.
PROiQ6IE14.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR017329. Pept_S1A_HAT/DESC1.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF037941. TMPRSS11ABCDE. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF82671. SSF82671. 1 hit.
PROSITEiPS50024. SEA. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTM11L_RAT
AccessioniPrimary (citable) accession number: Q6IE14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 94 of the entry and version 1 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.