Q9UL52 (TM11E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transmembrane protease serine 11E
EC=3.4.21.-

Alternative name(s):
Serine protease DESC1
Transmembrane protease serine 11E2

Cleaved into the following 2 chains:

1. Transmembrane protease serine 11E non-catalytic chain
2. Transmembrane protease serine 11E catalytic chain

Gene names

Name:	TMPRSS11E
Synonyms:	DESC1, TMPRSS11E2
ORF Names:	UNQ742/PRO1461

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type peptidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 191

191

Transmembrane protease serine 11E non-catalytic chain Potential

PRO_0000027891

Chain

192 – 423

232

Transmembrane protease serine 11E catalytic chain Potential

PRO_0000027892

Regions

Topological domain

1 – 19

19

Cytoplasmic Potential

Transmembrane

20 – 40

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

41 – 423

383

Extracellular Potential

Domain

44 – 165

122

SEA

Domain

192 – 422

231

Peptidase S1

Sites

Active site

232

1

Charge relay system Ref.6

Active site

277

1

Charge relay system Ref.6

Active site

373

1

Charge relay system Ref.6

Amino acid modifications

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

166

1

N-linked (GlcNAc...) Potential

Glycosylation

223

1

N-linked (GlcNAc...) Potential

Disulfide bond

177 ↔ 297

Interchain (between non-catalytic and catalytic chains) By similarity

Disulfide bond

217 ↔ 233

Ref.6

Disulfide bond

342 ↔ 358

Ref.6

Disulfide bond

369 ↔ 398

Ref.6

Natural variations

Natural variant

303

1

Y → C.
Corresponds to variant rs976002 [ dbSNP | Ensembl ].

VAR_051847

Experimental info

Sequence conflict

158

1

H → Q in AC019173. Ref.3

Secondary structure

1

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423

Helix Strand Turn

Details...

Beta strand

206 – 211

6

Beta strand

214 – 223

10

Beta strand

226 – 229

4

Helix

231 – 234

4

Helix

240 – 242

3

Beta strand

243 – 251

9

Beta strand

255 – 265

11

Beta strand

279 – 285

7

Beta strand

291 – 293

3

Beta strand

310 – 316

7

Beta strand

330 – 337

8

Helix

339 – 342

4

Turn

345 – 350

6

Beta strand

356 – 360

5

Beta strand

365 – 367

3

Beta strand

376 – 380

5

Beta strand

386 – 394

9

Beta strand

396 – 400

5

Beta strand

405 – 409

5

Helix

411 – 413

3

Helix

414 – 421

8

Sequences

	Sequence		Length	Mass (Da)
	Q9UL52 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: EB1476807C0B613D	FASTA	423	47,696
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00297030.

RefSeq

NP_054777.2. NM_014058.3.

UniGene

Hs.201877.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OQ5	X-ray	1.61	A	192-423	[»]

ProteinModelPortal

Q9UL52.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000307519.

Protein family/group databases

MEROPS

S01.021.

PTM databases

PhosphoSite

Q9UL52.

Polymorphism databases

DMDM

57015324.

Proteomic databases

PaxDb

Q9UL52.

PRIDE

Q9UL52.

Protocols and materials databases

DNASU

28983.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305363; ENSP00000307519; ENSG00000087128.

GeneID

28983.

KEGG

hsa:28983.

UCSC

uc003hdz.4. human.

Organism-specific databases

CTD

28983.

GeneCards

GC04P069313.

HGNC

HGNC:24465. TMPRSS11E.

HPA

HPA051062.

MIM

610399. gene.

neXtProt

NX_Q9UL52.

PharmGKB

PA142670729.
PA162406637.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOGENOM

HOG000251823.

HOVERGEN

HBG013304.

InParanoid

A6NL71.

KO

K09642.

OMA

AHMLLIF.

OrthoDB

EOG4XD3R4.

PhylomeDB

Q9UL52.

Gene expression databases

ArrayExpress

Q9UL52.

Bgee

Q9UL52.

CleanEx

HS_TMPRSS11E.

Genevestigator

Q9UL52.

GermOnline

ENSG00000087128. Homo sapiens.

Family and domain databases

InterPro

IPR017329. Pept_S1A_HAT/DESC1.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF037941. TMPRSS11ABCDE. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50024. SEA. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UL52.

GenomeRNAi

28983.

NextBio

51877.

SOURCE

Search...

Entry information

Entry name

TM11E_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.