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Protein

Transmembrane protease serine 11B-like protein

Gene

Tmprss11b

Organism
Mus musculus (Mouse)
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 sitei225 – 2251Charge relay systemBy similarity
Active sitei270 – 2701Charge relay systemBy similarity
Active sitei366 – 3661Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.207.

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:Tmprss11b
Synonyms:Hatl5, Tmprss11bnl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2442893. Tmprss11b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence analysisAdd
BLAST
Transmembranei16 – 3621Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini37 – 416380ExtracellularSequence 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 – 416416Transmembrane protease serine 11B-like proteinPRO_0000299320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi210 ↔ 226PROSITE-ProRule annotation
Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi335 ↔ 351PROSITE-ProRule annotation
Disulfide bondi362 ↔ 391PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ14C59.
PRIDEiQ14C59.

Expressioni

Tissue specificityi

Expressed in esophagus, cervix, tongue, and testes.1 Publication

Gene expression databases

BgeeiQ14C59.
CleanExiMM_TMPRSS11B.

Structurei

3D structure databases

ProteinModelPortaliQ14C59.
SMRiQ14C59. Positions 44-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 161118SEAPROSITE-ProRule annotationAdd
BLAST
Domaini185 – 415231Peptidase 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

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251823.
HOVERGENiHBG013304.
InParanoidiQ14C59.
KOiK09751.
OMAiIINNRCG.
OrthoDBiEOG75B84T.
PhylomeDBiQ14C59.
TreeFamiTF351684.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR017329. Pept_S1A_HAT/DESC1.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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.

Q14C59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRPVIASRK SIPPWLIILC VLGVLAALGI IIGLLVHFLA VENKIYYYQG
60 70 80 90 100
GFKVLDIPYD RNYERETSLE SNYLSKILEN KMVEAFQNSN IYKQYINSQV
110 120 130 140 150
ITLVPDNNSV TAHIWLVFKD PWSNKENLRR RIESILRQML ENNPESLTTD
160 170 180 190 200
PGSLKLTEIS KVDAEKIINN RCGRRPRMSA TYDRITGGST AHKGEWPWQA
210 220 230 240 250
SLRVNGKHYC GASLIGERFL LTAAHCFQGT NNPKNLTVSF GTRVTPAYMQ
260 270 280 290 300
HSVQEIIIHE DYVKGEHHDD VAVIKLTEKV SFNNDVHRVC LPESTQIFPP
310 320 330 340 350
GEGVVVTGWG SFSYNGKSPL LLQKASIKII DTNTCNSEEA YGGRIVDTML
360 370 380 390 400
CAGYLEGSID ACQGDSGGPL VHPNSRDIWY LVGIVSWGHE CGRVNKPGVY
410
MRVTSYRNWI ASKTGI
Length:416
Mass (Da):46,713
Last modified:September 11, 2007 - v2
Checksum:i5185C42C39BAB9F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561D → N in AAI15420 (PubMed:15489334).Curated
Sequence conflicti98 – 981S → Y in BAC29606 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036858 mRNA. Translation: BAC29606.1.
AK036968 mRNA. Translation: BAC29652.1.
AK137654 mRNA. Translation: BAE23447.1.
BC115419 mRNA. Translation: AAI15420.1.
BC115420 mRNA. Translation: AAI15421.1.
CCDSiCCDS39126.1.
RefSeqiNP_795998.2. NM_177024.4.
UniGeneiMm.253994.

Genome annotation databases

EnsembliENSMUST00000038448; ENSMUSP00000042406; ENSMUSG00000035861.
GeneIDi319875.
KEGGimmu:319875.
UCSCiuc008xxu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036858 mRNA. Translation: BAC29606.1.
AK036968 mRNA. Translation: BAC29652.1.
AK137654 mRNA. Translation: BAE23447.1.
BC115419 mRNA. Translation: AAI15420.1.
BC115420 mRNA. Translation: AAI15421.1.
CCDSiCCDS39126.1.
RefSeqiNP_795998.2. NM_177024.4.
UniGeneiMm.253994.

3D structure databases

ProteinModelPortaliQ14C59.
SMRiQ14C59. Positions 44-416.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.207.

Proteomic databases

PaxDbiQ14C59.
PRIDEiQ14C59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038448; ENSMUSP00000042406; ENSMUSG00000035861.
GeneIDi319875.
KEGGimmu:319875.
UCSCiuc008xxu.1. mouse.

Organism-specific databases

CTDi132724.
MGIiMGI:2442893. Tmprss11b.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251823.
HOVERGENiHBG013304.
InParanoidiQ14C59.
KOiK09751.
OMAiIINNRCG.
OrthoDBiEOG75B84T.
PhylomeDBiQ14C59.
TreeFamiTF351684.

Miscellaneous databases

NextBioi395565.
PROiQ14C59.
SOURCEiSearch...

Gene expression databases

BgeeiQ14C59.
CleanExiMM_TMPRSS11B.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR017329. Pept_S1A_HAT/DESC1.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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. "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.
    Tissue: Vagina.
  2. "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].
  3. "Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes."
    Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C., Strickland D.K., Lawrence D.A., Antalis T.M., Bugge T.H.
    J. Biol. Chem. 279:46981-46994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. "HATL5: a cell surface serine protease differentially expressed in epithelial cancers."
    Miller G.S., Zoratti G.L., Murray A.S., Bergum C., Tanabe L.M., List K.
    PLoS ONE 9:E87675-E87675(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiTM11B_MOUSE
AccessioniPrimary (citable) accession number: Q14C59
Secondary accession number(s): Q8BZ13, Q8BZ30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: May 11, 2016
This is version 80 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. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.