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Q9Y5Y6 (ST14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. 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:
Suppressor of tumorigenicity 14 protein

EC=3.4.21.109
Alternative name(s):
Matriptase
Membrane-type serine protease 1
Short name=MT-SP1
Prostamin
Serine protease 14
Serine protease TADG-15
Tumor-associated differentially-expressed gene 15 protein
Gene names
Name:ST14
Synonyms:PRSS14, SNC19, TADG15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length855 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site.

Catalytic activity

Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position. Ref.9

Subunit structure

Interacts with CDCP1. May interact with TMEFF1. Ref.8 Ref.9

Subcellular location

Membrane; Single-pass type II membrane protein Probable.

Involvement in disease

Ichthyosis, autosomal recessive, with hypotrichosis (ARIH) [MIM:610765]: A skin disorder characterized by congenital ichthyosis associated with the presence of less than the normal amount of hair.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 CUB domains.

Contains 4 LDL-receptor class A domains.

Contains 1 peptidase S1 domain.

Contains 1 SEA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 855855Suppressor of tumorigenicity 14 protein
PRO_0000088712

Regions

Topological domain1 – 5555Cytoplasmic Potential
Transmembrane56 – 7621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain77 – 855779Extracellular Potential
Domain86 – 203118SEA
Domain214 – 334121CUB 1
Domain340 – 447108CUB 2
Domain452 – 48736LDL-receptor class A 1
Domain487 – 52438LDL-receptor class A 2
Domain524 – 56037LDL-receptor class A 3
Domain566 – 60338LDL-receptor class A 4
Domain615 – 854240Peptidase S1

Sites

Active site6561Charge relay system
Active site7111Charge relay system
Active site8051Charge relay system

Amino acid modifications

Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation7721N-linked (GlcNAc...) Potential
Disulfide bond214 ↔ 244 By similarity
Disulfide bond340 ↔ 366 By similarity
Disulfide bond397 ↔ 410 By similarity
Disulfide bond453 ↔ 464 By similarity
Disulfide bond459 ↔ 477 By similarity
Disulfide bond471 ↔ 486 By similarity
Disulfide bond488 ↔ 501 By similarity
Disulfide bond496 ↔ 514 By similarity
Disulfide bond508 ↔ 523 By similarity
Disulfide bond525 ↔ 537 By similarity
Disulfide bond532 ↔ 550 By similarity
Disulfide bond544 ↔ 559 By similarity
Disulfide bond567 ↔ 579 By similarity
Disulfide bond574 ↔ 593 By similarity
Disulfide bond587 ↔ 602 By similarity
Disulfide bond641 ↔ 657 Ref.11
Disulfide bond776 ↔ 790 Ref.11
Disulfide bond801 ↔ 830 Ref.11

Natural variations

Natural variant2851M → I.
Corresponds to variant rs7126904 [ dbSNP | Ensembl ].
VAR_032847
Natural variant3811R → S. Ref.4
Corresponds to variant rs17667603 [ dbSNP | Ensembl ].
VAR_032848
Natural variant8271G → R in ARIH. Ref.12
VAR_032849

Experimental info

Mutagenesis6561H → A: Abolishes catalytic activity. Ref.9
Mutagenesis7111D → A: Abolishes catalytic activity. Ref.9
Mutagenesis8051S → A: Abolishes catalytic activity. Ref.9
Sequence conflict6741A → V in BAB20376. Ref.3

Secondary structure

............................................ 855
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y5Y6 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: 26143132C01F99C9

FASTA85594,770
        10         20         30         40         50         60 
MGSDRARKGG GGPKDFGAGL KYNSRHEKVN GLEEGVEFLP VNNVKKVEKH GPGRWVVLAA 

        70         80         90        100        110        120 
VLIGLLLVLL GIGFLVWHLQ YRDVRVQKVF NGYMRITNEN FVDAYENSNS TEFVSLASKV 

       130        140        150        160        170        180 
KDALKLLYSG VPFLGPYHKE SAVTAFSEGS VIAYYWSEFS IPQHLVEEAE RVMAEERVVM 

       190        200        210        220        230        240 
LPPRARSLKS FVVTSVVAFP TDSKTVQRTQ DNSCSFGLHA RGVELMRFTT PGFPDSPYPA 

       250        260        270        280        290        300 
HARCQWALRG DADSVLSLTF RSFDLASCDE RGSDLVTVYN TLSPMEPHAL VQLCGTYPPS 

       310        320        330        340        350        360 
YNLTFHSSQN VLLITLITNT ERRHPGFEAT FFQLPRMSSC GGRLRKAQGT FNSPYYPGHY 

       370        380        390        400        410        420 
PPNIDCTWNI EVPNNQHVKV RFKFFYLLEP GVPAGTCPKD YVEINGEKYC GERSQFVVTS 

       430        440        450        460        470        480 
NSNKITVRFH SDQSYTDTGF LAEYLSYDSS DPCPGQFTCR TGRCIRKELR CDGWADCTDH 

       490        500        510        520        530        540 
SDELNCSCDA GHQFTCKNKF CKPLFWVCDS VNDCGDNSDE QGCSCPAQTF RCSNGKCLSK 

       550        560        570        580        590        600 
SQQCNGKDDC GDGSDEASCP KVNVVTCTKH TYRCLNGLCL SKGNPECDGK EDCSDGSDEK 

       610        620        630        640        650        660 
DCDCGLRSFT RQARVVGGTD ADEGEWPWQV SLHALGQGHI CGASLISPNW LVSAAHCYID 

       670        680        690        700        710        720 
DRGFRYSDPT QWTAFLGLHD QSQRSAPGVQ ERRLKRIISH PFFNDFTFDY DIALLELEKP 

       730        740        750        760        770        780 
AEYSSMVRPI CLPDASHVFP AGKAIWVTGW GHTQYGGTGA LILQKGEIRV INQTTCENLL 

       790        800        810        820        830        840 
PQQITPRMMC VGFLSGGVDS CQGDSGGPLS SVEADGRIFQ AGVVSWGDGC AQRNKPGVYT 

       850 
RLPLFRDWIK ENTGV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity."
Lin C.Y., Anders J., Johnson M., Sang Q.A., Dickson R.B.
J. Biol. Chem. 274:18231-18236(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue."
Takeuchi T., Shuman M.A., Craik C.S.
Proc. Natl. Acad. Sci. U.S.A. 96:11054-11061(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular cloning of a novel transmembrane serine protease expressed in human prostate."
Yamaguchi N., Mitsui S.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Prostate.
[4]Tanimoto H., Underwood L.J., Wang Y., Shigemasa K., Parmley T.H., O'Brien T.J.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-381.
[5]"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: Blood and Muscle.
[6]"Genomic analysis of a novel human serine protease SNC19."
Cao J., Fan W., Zheng S.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-664.
[7]"Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk."
Lin C.Y., Anders J., Johnson M., Dickson R.B.
J. Biol. Chem. 274:18237-18242(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Milk.
[8]"Adhesion signaling by a novel mitotic substrate of src kinases."
Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.
Oncogene 24:5333-5343(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDCP1.
[9]"Protein interaction analysis of ST14 domains and their point and deletion mutants."
Ge W., Hu H., Ding K., Sun L., Zheng S.
J. Biol. Chem. 281:7406-7412(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-656; ASP-711 AND SER-805, POSSIBLE INTERACTION WITH TMEFF1.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase."
Friedrich R., Fuentes-Prior P., Ong E., Coombs G., Hunter M., Oehler R., Pierson D., Gonzalez R., Huber R., Bode W., Madison E.L.
J. Biol. Chem. 277:2160-2168(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 615-855 IN COMPLEX WITH INHIBITORS, DISULFIDE BONDS.
[12]"Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase."
Basel-Vanagaite L., Attia R., Ishida-Yamamoto A., Rainshtein L., Ben Amitai D., Lurie R., Pasmanik-Chor M., Indelman M., Zvulunov A., Saban S., Magal N., Sprecher E., Shohat M.
Am. J. Hum. Genet. 80:467-477(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARIH ARG-827.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF118224 mRNA. Translation: AAD42765.2.
AF133086 mRNA. Translation: AAF00109.1.
AB030036 mRNA. Translation: BAB20376.1.
AF057145 mRNA. Translation: AAG15395.1.
BC005826 mRNA. Translation: AAH05826.2.
BC030532 mRNA. Translation: AAH30532.1.
AF283256 Genomic DNA. Translation: AAG13949.1.
CCDSCCDS8487.1.
RefSeqNP_068813.1. NM_021978.3.
UniGeneHs.504315.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EAWX-ray2.93A/C615-855[»]
1EAXX-ray1.30A615-855[»]
2FMVmodel-A214-447[»]
2GV6X-ray2.10A615-855[»]
2GV7X-ray2.20A615-855[»]
3BN9X-ray2.17A/B615-855[»]
3NCLX-ray1.19A615-855[»]
3NPSX-ray1.50A615-855[»]
3P8FX-ray2.00A615-855[»]
3P8GX-ray1.20A615-855[»]
3SO3X-ray2.10A615-855[»]
4IS5X-ray1.48A615-855[»]
4ISLX-ray2.29A615-855[»]
4ISNX-ray2.45A615-855[»]
4ISOX-ray2.01A615-855[»]
4JYTX-ray2.00A615-855[»]
4JZ1X-ray1.90A615-855[»]
4JZIX-ray2.00A615-855[»]
ProteinModelPortalQ9Y5Y6.
SMRQ9Y5Y6. Positions 228-855.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112645. 4 interactions.
IntActQ9Y5Y6. 3 interactions.
MINTMINT-6784312.
STRING9606.ENSP00000278742.

Chemistry

BindingDBQ9Y5Y6.
ChEMBLCHEMBL3018.
DrugBankDB00013. Urokinase.

Protein family/group databases

MEROPSS01.302.

PTM databases

PhosphoSiteQ9Y5Y6.

Polymorphism databases

DMDM13124575.

Proteomic databases

MaxQBQ9Y5Y6.
PaxDbQ9Y5Y6.
PeptideAtlasQ9Y5Y6.
PRIDEQ9Y5Y6.

Protocols and materials databases

DNASU6768.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278742; ENSP00000278742; ENSG00000149418.
GeneID6768.
KEGGhsa:6768.
UCSCuc001qfw.3. human.

Organism-specific databases

CTD6768.
GeneCardsGC11P130063.
HGNCHGNC:11344. ST14.
MIM606797. gene.
610765. phenotype.
neXtProtNX_Q9Y5Y6.
Orphanet91132. Ichthyosis-hypotrichosis syndrome.
PharmGKBPA36168.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000136851.
HOVERGENHBG012556.
InParanoidQ9Y5Y6.
KOK08670.
OMADSSDPCP.
OrthoDBEOG75B84T.
PhylomeDBQ9Y5Y6.
TreeFamTF330647.

Enzyme and pathway databases

BRENDA3.4.21.109. 2681.

Gene expression databases

ArrayExpressQ9Y5Y6.
BgeeQ9Y5Y6.
CleanExHS_ST14.
GenevestigatorQ9Y5Y6.

Family and domain databases

Gene3D2.60.120.290. 2 hits.
4.10.400.10. 4 hits.
InterProIPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR017051. Peptidase_S1A_matripase.
IPR000082. SEA_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00431. CUB. 2 hits.
PF00057. Ldl_recept_a. 4 hits.
PF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF036370. ST14. 1 hit.
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00042. CUB. 2 hits.
SM00192. LDLa. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57424. SSF57424. 4 hits.
SSF82671. SSF82671. 1 hit.
PROSITEPS01180. CUB. 2 hits.
PS01209. LDLRA_1. 3 hits.
PS50068. LDLRA_2. 4 hits.
PS50024. SEA. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSST14. human.
EvolutionaryTraceQ9Y5Y6.
GenomeRNAi6768.
NextBio26412.
PMAP-CutDBQ9Y5Y6.
PROQ9Y5Y6.
SOURCESearch...

Entry information

Entry nameST14_HUMAN
AccessionPrimary (citable) accession number: Q9Y5Y6
Secondary accession number(s): Q9BS01 expand/collapse secondary AC list , Q9H3S0, Q9HB36, Q9HCA3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 146 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 11

Human chromosome 11: entries, gene names and cross-references to MIM