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Protein

Suppressor of tumorigenicity 14 protein homolog

Gene

St14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degrades extracellular matrix. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site (By similarity). Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing (By similarity).By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei656 – 6561Charge relay systemBy similarity
Active sitei711 – 7111Charge relay systemBy similarity
Active sitei805 – 8051Charge relay systemBy similarity

GO - Molecular functioni

  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: MGI

GO - Biological processi

  • cell migration Source: MGI
  • epithelial cell morphogenesis involved in placental branching Source: MGI
  • keratinocyte differentiation Source: UniProtKB
  • neural tube closure Source: MGI
  • proteolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.302.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of tumorigenicity 14 protein homolog (EC:3.4.21.109)
Alternative name(s):
Epithin
Serine protease 14
Gene namesi
Name:St14
Synonyms:Prss14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1338881. St14.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555CytoplasmicSequence analysisAdd
BLAST
Transmembranei56 – 7621Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini77 – 855779ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: Ensembl
  • extracellular exosome Source: MGI
  • extracellular region Source: MGI
  • extracellular space Source: Ensembl
  • extrinsic component of plasma membrane Source: MGI
  • integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 855855Suppressor of tumorigenicity 14 protein homologPRO_0000088713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineCombined sources
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi214 ↔ 244By similarity
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi340 ↔ 366By similarity
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi397 ↔ 410By similarity
Glycosylationi421 – 4211N-linked (GlcNAc...)1 Publication
Disulfide bondi453 ↔ 464By similarity
Disulfide bondi459 ↔ 477By similarity
Disulfide bondi471 ↔ 486By similarity
Disulfide bondi488 ↔ 501By similarity
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence analysis
Disulfide bondi496 ↔ 514By similarity
Disulfide bondi508 ↔ 523By similarity
Disulfide bondi525 ↔ 537By similarity
Disulfide bondi532 ↔ 550By similarity
Disulfide bondi544 ↔ 559By similarity
Disulfide bondi567 ↔ 579By similarity
Disulfide bondi574 ↔ 593By similarity
Disulfide bondi587 ↔ 602By similarity
Disulfide bondi641 ↔ 657By similarity
Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence analysis
Disulfide bondi776 ↔ 790By similarity
Disulfide bondi801 ↔ 830By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP56677.
PaxDbiP56677.
PeptideAtlasiP56677.
PRIDEiP56677.

PTM databases

iPTMnetiP56677.
PhosphoSiteiP56677.

Expressioni

Tissue specificityi

Highly expressed in intestine, kidney, lung, and thymus. Not expressed in skeletal muscle, liver, heart, testis and brain.

Gene expression databases

BgeeiP56677.
ExpressionAtlasiP56677. baseline and differential.
GenevisibleiP56677. MM.

Interactioni

Subunit structurei

Interacts with CDCP1. May interact with TMEFF1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034478.

Structurei

3D structure databases

ProteinModelPortaliP56677.
SMRiP56677. Positions 228-855.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 203118SEAPROSITE-ProRule annotationAdd
BLAST
Domaini214 – 331118CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini340 – 444105CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini451 – 48838LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini489 – 52234LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini523 – 56139LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini565 – 60440LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini615 – 854240Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 4 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SEA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000136851.
HOVERGENiHBG012556.
InParanoidiP56677.
KOiK08670.
OMAiMMCVGFL.
OrthoDBiEOG75B84T.
PhylomeDBiP56677.
TreeFamiTF330647.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
4.10.400.10. 4 hits.
InterProiIPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR017051. Peptidase_S1A_matripase.
IPR000082. SEA_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00057. Ldl_recept_a. 4 hits.
PF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF036370. ST14. 1 hit.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00042. CUB. 2 hits.
SM00192. LDLa. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57424. SSF57424. 4 hits.
SSF82671. SSF82671. 1 hit.
PROSITEiPS01180. 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]

Sequencei

Sequence statusi: Complete.

P56677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSNRGRKAG GGSQDFGAGL KYNSRLENMN GFEEGVEFLP ANNAKKVEKR
60 70 80 90 100
GPRRWVVLVA VLFSFLLLSL MAGLLVWHFH YRNVRVQKVF NGHLRITNEI
110 120 130 140 150
FLDAYENSTS TEFISLASQV KEALKLLYNE VPVLGPYHKK SAVTAFSEGS
160 170 180 190 200
VIAYYWSEFS IPPHLAEEVD RAMAVERVVT LPPRARALKS FVLTSVVAFP
210 220 230 240 250
IDPRMLQRTQ DNSCSFALHA HGAAVTRFTT PGFPNSPYPA HARCQWVLRG
260 270 280 290 300
DADSVLSLTF RSFDVAPCDE HGSDLVTVYD SLSPMEPHAV VRLCGTFSPS
310 320 330 340 350
YNLTFLSSQN VFLVTLITNT DRRHPGFEAT FFQLPKMSSC GGFLSDTQGT
360 370 380 390 400
FSSPYYPGHY PPNINCTWNI KVPNNRNVKV RFKLFYLVDP NVPVGSCTKD
410 420 430 440 450
YVEINGEKYC GERSQFVVSS NSSKITVHFH SDHSYTDTGF LAEYLSYDSN
460 470 480 490 500
DPCPGMFMCK TGRCIRKELR CDGWADCPDY SDERYCRCNA THQFTCKNQF
510 520 530 540 550
CKPLFWVCDS VNDCGDGSDE EGCSCPAGSF KCSNGKCLPQ SQKCNGKDNC
560 570 580 590 600
GDGSDEASCD SVNVVSCTKY TYRCQNGLCL SKGNPECDGK TDCSDGSDEK
610 620 630 640 650
NCDCGLRSFT KQARVVGGTN ADEGEWPWQV SLHALGQGHL CGASLISPDW
660 670 680 690 700
LVSAAHCFQD DKNFKYSDYT MWTAFLGLLD QSKRSASGVQ ELKLKRIITH
710 720 730 740 750
PSFNDFTFDY DIALLELEKS VEYSTVVRPI CLPDATHVFP AGKAIWVTGW
760 770 780 790 800
GHTKEGGTGA LILQKGEIRV INQTTCEDLM PQQITPRMMC VGFLSGGVDS
810 820 830 840 850
CQGDSGGPLS SAEKDGRMFQ AGVVSWGEGC AQRNKPGVYT RLPVVRDWIK

EHTGV
Length:855
Mass (Da):94,655
Last modified:May 4, 2001 - v2
Checksum:i4F10E84DA2146DD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042822 mRNA. Translation: AAD02230.3.
BC005496 mRNA. Translation: AAH05496.1.
CCDSiCCDS22948.1.
RefSeqiNP_035306.2. NM_011176.4.
UniGeneiMm.243926.

Genome annotation databases

EnsembliENSMUST00000034478; ENSMUSP00000034478; ENSMUSG00000031995.
GeneIDi19143.
KEGGimmu:19143.
UCSCiuc009ori.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042822 mRNA. Translation: AAD02230.3.
BC005496 mRNA. Translation: AAH05496.1.
CCDSiCCDS22948.1.
RefSeqiNP_035306.2. NM_011176.4.
UniGeneiMm.243926.

3D structure databases

ProteinModelPortaliP56677.
SMRiP56677. Positions 228-855.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034478.

Protein family/group databases

MEROPSiS01.302.

PTM databases

iPTMnetiP56677.
PhosphoSiteiP56677.

Proteomic databases

EPDiP56677.
PaxDbiP56677.
PeptideAtlasiP56677.
PRIDEiP56677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034478; ENSMUSP00000034478; ENSMUSG00000031995.
GeneIDi19143.
KEGGimmu:19143.
UCSCiuc009ori.1. mouse.

Organism-specific databases

CTDi6768.
MGIiMGI:1338881. St14.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000136851.
HOVERGENiHBG012556.
InParanoidiP56677.
KOiK08670.
OMAiMMCVGFL.
OrthoDBiEOG75B84T.
PhylomeDBiP56677.
TreeFamiTF330647.

Miscellaneous databases

PROiP56677.
SOURCEiSearch...

Gene expression databases

BgeeiP56677.
ExpressionAtlasiP56677. baseline and differential.
GenevisibleiP56677. MM.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
4.10.400.10. 4 hits.
InterProiIPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR017051. Peptidase_S1A_matripase.
IPR000082. SEA_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00057. Ldl_recept_a. 4 hits.
PF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF036370. ST14. 1 hit.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00042. CUB. 2 hits.
SM00192. LDLa. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57424. SSF57424. 4 hits.
SSF82671. SSF82671. 1 hit.
PROSITEiPS01180. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains."
    Kim M.G., Chen C., Lyu M.S., Cho E.G., Park D., Kozak C., Schwartz R.H.
    Immunogenetics 49:420-428(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C.B.17SCID.
    Tissue: Thymus.
  2. Kim M.G., Chen C., Cho E.G., Park D., Schwartz R.H.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 23; 321; 325; 343; 409-410 AND C-TERMINUS.
  3. "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: Mammary tumor.
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-421.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Pancreas.

Entry informationi

Entry nameiST14_MOUSE
AccessioniPrimary (citable) accession number: P56677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 4, 2001
Last modified: July 6, 2016
This is version 153 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.