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Q9UL52 (TM11E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 11E

EC=3.4.21.-
Alternative name(s):
Serine protease DESC1
Transmembrane protease serine 11E2
Gene names
Name:TMPRSS11E
Synonyms:DESC1, TMPRSS11E2
ORF Names:UNQ742/PRO1461
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position By similarity.

Enzyme regulation

Inhibited by SERPINA5. Ref.5

Subunit structure

Forms a heterodimer with SERPINA5 and SERPINE1.

Subcellular location

Cell membrane; Single-pass type II membrane protein By similarity.

Transmembrane protease serine 11E catalytic chain: Secreted By similarity. Note: Activated by cleavage and secreted By similarity.

Tissue specificity

Expression can only be detected in tissues derived from the head and neck, and in skin, prostate and testis. Ref.1

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 1 SEA domain.

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191Transmembrane protease serine 11E non-catalytic chain Potential
PRO_0000027891
Chain192 – 423232Transmembrane protease serine 11E catalytic chain Potential
PRO_0000027892

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 4021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain41 – 423383Extracellular Potential
Domain49 – 167119SEA
Domain192 – 422231Peptidase S1

Sites

Active site2321Charge relay system Ref.6
Active site2771Charge relay system Ref.6
Active site3731Charge relay system Ref.6

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Disulfide bond177 ↔ 297Interchain (between non-catalytic and catalytic chains) By similarity
Disulfide bond217 ↔ 233 Ref.6
Disulfide bond342 ↔ 358 Ref.6
Disulfide bond369 ↔ 398 Ref.6

Natural variations

Natural variant3031Y → C.
Corresponds to variant rs976002 [ dbSNP | Ensembl ].
VAR_051847

Experimental info

Sequence conflict1581H → Q in AC019173. Ref.3

Secondary structure

......................................... 423
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UL52 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: EB1476807C0B613D

FASTA42347,696
        10         20         30         40         50         60 
MMYRPDVVRA RKRVCWEPWV IGLVIFISLI VLAVCIGLTV HYVRYNQKKT YNYYSTLSFT 

        70         80         90        100        110        120 
TDKLYAEFGR EASNNFTEMS QRLESMVKNA FYKSPLREEF VKSQVIKFSQ QKHGVLAHML 

       130        140        150        160        170        180 
LICRFHSTED PETVDKIVQL VLHEKLQDAV GPPKVDPHSV KIKKINKTET DSYLNHCCGT 

       190        200        210        220        230        240 
RRSKTLGQSL RIVGGTEVEE GEWPWQASLQ WDGSHRCGAT LINATWLVSA AHCFTTYKNP 

       250        260        270        280        290        300 
ARWTASFGVT IKPSKMKRGL RRIIVHEKYK HPSHDYDISL AELSSPVPYT NAVHRVCLPD 

       310        320        330        340        350        360 
ASYEFQPGDV MFVTGFGALK NDGYSQNHLR QAQVTLIDAT TCNEPQAYND AITPRMLCAG 

       370        380        390        400        410        420 
SLEGKTDACQ GDSGGPLVSS DARDIWYLAG IVSWGDECAK PNKPGVYTRV TALRDWITSK 


TGI 

« Hide

References

« Hide 'large scale' references
[1]"Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck."
Lang J.C., Schuller D.E.
Br. J. Cancer 84:237-243(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Brain.
[5]"Regulation of carcinoma cell invasion by protein C inhibitor whose expression is decreased in renal cell carcinoma."
Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K., Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.
Int. J. Cancer 108:516-523(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
[6]"Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family."
Kyrieleis O.J., Huber R., Ong E., Oehler R., Hunter M., Madison E.L., Jacob U.
FEBS J. 274:2148-2160(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 192-423, ACTIVE SITE, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064819 mRNA. Translation: AAF04328.1.
AY359017 mRNA. Translation: AAQ89376.1.
AC140484 Genomic DNA. No translation available.
AC019173 Genomic DNA. No translation available.
BC113412 mRNA. Translation: AAI13413.1.
BC113414 mRNA. Translation: AAI13415.1.
RefSeqNP_054777.2. NM_014058.3.
UniGeneHs.201877.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OQ5X-ray1.61A192-423[»]
ProteinModelPortalQ9UL52.
SMRQ9UL52. Positions 48-124, 164-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000307519.

Protein family/group databases

MEROPSS01.021.

PTM databases

PhosphoSiteQ9UL52.

Polymorphism databases

DMDM57015324.

Proteomic databases

PaxDbQ9UL52.
PRIDEQ9UL52.

Protocols and materials databases

DNASU28983.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305363; ENSP00000307519; ENSG00000087128.
GeneID28983.
KEGGhsa:28983.
UCSCuc003hdz.4. human.

Organism-specific databases

CTD28983.
GeneCardsGC04P069313.
HGNCHGNC:24465. TMPRSS11E.
HPAHPA051062.
MIM610399. gene.
neXtProtNX_Q9UL52.
PharmGKBPA142670729.
PA162406637.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251823.
HOVERGENHBG013304.
InParanoidA6NL71.
KOK09642.
OMAYEGISKC.
OrthoDBEOG75B84T.
PhylomeDBQ9UL52.
TreeFamTF351684.

Gene expression databases

ArrayExpressQ9UL52.
BgeeQ9UL52.
CleanExHS_TMPRSS11E.
GenevestigatorQ9UL52.

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

EvolutionaryTraceQ9UL52.
GenomeRNAi28983.
NextBio51877.
PROQ9UL52.
SOURCESearch...

Entry information

Entry nameTM11E_HUMAN
AccessionPrimary (citable) accession number: Q9UL52
Secondary accession number(s): A6NL71, Q14DC8, Q6UW31
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 4, 2005
Last modified: March 19, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM