ST14_MOUSE
ID ST14_MOUSE Reviewed; 855 AA.
AC P56677;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Suppressor of tumorigenicity 14 protein homolog;
DE EC=3.4.21.109;
DE AltName: Full=Epithin;
DE AltName: Full=Serine protease 14;
GN Name=St14; Synonyms=Prss14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C.B.17SCID; TISSUE=Thymus;
RX PubMed=10199918; DOI=10.1007/s002510050515;
RA Kim M.G., Chen C., Lyu M.S., Cho E.G., Park D., Kozak C., Schwartz R.H.;
RT "Cloning and chromosomal mapping of a gene isolated from thymic stromal
RT cells encoding a new mouse type II membrane serine protease, epithin,
RT containing four LDL receptor modules and two CUB domains.";
RL Immunogenetics 49:420-428(1999).
RN [2]
RP SEQUENCE REVISION TO 23; 321; 325; 343; 409-410 AND C-TERMINUS.
RA Kim M.G., Chen C., Cho E.G., Park D., Schwartz R.H.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-421.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Degrades extracellular matrix. Exhibits trypsin-like activity
CC as defined by cleavage of synthetic substrates with Arg or Lys as the
CC P1 site (By similarity). Involved in the terminal differentiation of
CC keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG)
CC processing (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves various synthetic substrates with Arg or Lys at the P1
CC position and prefers small side-chain amino acids, such as Ala and
CC Gly, at the P2 position.; EC=3.4.21.109;
CC -!- SUBUNIT: Interacts with CDCP1. May interact with TMEFF1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in intestine, kidney, lung, and
CC thymus. Not expressed in skeletal muscle, liver, heart, testis and
CC brain.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF042822; AAD02230.3; -; mRNA.
DR EMBL; BC005496; AAH05496.1; -; mRNA.
DR CCDS; CCDS22948.1; -.
DR RefSeq; NP_035306.2; NM_011176.4.
DR AlphaFoldDB; P56677; -.
DR SMR; P56677; -.
DR STRING; 10090.ENSMUSP00000034478; -.
DR BindingDB; P56677; -.
DR ChEMBL; CHEMBL3745587; -.
DR MEROPS; S01.302; -.
DR GlyGen; P56677; 6 sites.
DR iPTMnet; P56677; -.
DR PhosphoSitePlus; P56677; -.
DR EPD; P56677; -.
DR PaxDb; P56677; -.
DR PeptideAtlas; P56677; -.
DR PRIDE; P56677; -.
DR ProteomicsDB; 257425; -.
DR Antibodypedia; 33087; 406 antibodies from 36 providers.
DR DNASU; 19143; -.
DR Ensembl; ENSMUST00000034478; ENSMUSP00000034478; ENSMUSG00000031995.
DR GeneID; 19143; -.
DR KEGG; mmu:19143; -.
DR UCSC; uc009ori.1; mouse.
DR CTD; 6768; -.
DR MGI; MGI:1338881; St14.
DR VEuPathDB; HostDB:ENSMUSG00000031995; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155418; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR InParanoid; P56677; -.
DR OMA; CTWDIQV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P56677; -.
DR TreeFam; TF330647; -.
DR BioGRID-ORCS; 19143; 0 hits in 74 CRISPR screens.
DR ChiTaRS; St14; mouse.
DR PRO; PR:P56677; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P56677; protein.
DR Bgee; ENSMUSG00000031995; Expressed in hair follicle and 168 other tissues.
DR ExpressionAtlas; P56677; baseline and differential.
DR Genevisible; P56677; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
DR GO; GO:0016477; P:cell migration; TAS:MGI.
DR GO; GO:0060672; P:epithelial cell morphogenesis involved in placental branching; IGI:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 3.30.70.960; -; 1.
DR Gene3D; 4.10.400.10; -; 4.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR017051; Peptidase_S1A_matripase.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036370; ST14; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57424; SSF57424; 4.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..855
FT /note="Suppressor of tumorigenicity 14 protein homolog"
FT /id="PRO_0000088713"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 86..203
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 214..331
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 340..444
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 451..488
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 489..522
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 523..561
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 565..604
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 615..854
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 656
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 711
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 805
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..244
FT /evidence="ECO:0000250"
FT DISULFID 340..366
FT /evidence="ECO:0000250"
FT DISULFID 397..410
FT /evidence="ECO:0000250"
FT DISULFID 453..464
FT /evidence="ECO:0000250"
FT DISULFID 459..477
FT /evidence="ECO:0000250"
FT DISULFID 471..486
FT /evidence="ECO:0000250"
FT DISULFID 488..501
FT /evidence="ECO:0000250"
FT DISULFID 496..514
FT /evidence="ECO:0000250"
FT DISULFID 508..523
FT /evidence="ECO:0000250"
FT DISULFID 525..537
FT /evidence="ECO:0000250"
FT DISULFID 532..550
FT /evidence="ECO:0000250"
FT DISULFID 544..559
FT /evidence="ECO:0000250"
FT DISULFID 567..579
FT /evidence="ECO:0000250"
FT DISULFID 574..593
FT /evidence="ECO:0000250"
FT DISULFID 587..602
FT /evidence="ECO:0000250"
FT DISULFID 641..657
FT /evidence="ECO:0000250"
FT DISULFID 776..790
FT /evidence="ECO:0000250"
FT DISULFID 801..830
FT /evidence="ECO:0000250"
SQ SEQUENCE 855 AA; 94655 MW; 4F10E84DA2146DD5 CRC64;
MGSNRGRKAG GGSQDFGAGL KYNSRLENMN GFEEGVEFLP ANNAKKVEKR GPRRWVVLVA
VLFSFLLLSL MAGLLVWHFH YRNVRVQKVF NGHLRITNEI FLDAYENSTS TEFISLASQV
KEALKLLYNE VPVLGPYHKK SAVTAFSEGS VIAYYWSEFS IPPHLAEEVD RAMAVERVVT
LPPRARALKS FVLTSVVAFP IDPRMLQRTQ DNSCSFALHA HGAAVTRFTT PGFPNSPYPA
HARCQWVLRG DADSVLSLTF RSFDVAPCDE HGSDLVTVYD SLSPMEPHAV VRLCGTFSPS
YNLTFLSSQN VFLVTLITNT DRRHPGFEAT FFQLPKMSSC GGFLSDTQGT FSSPYYPGHY
PPNINCTWNI KVPNNRNVKV RFKLFYLVDP NVPVGSCTKD YVEINGEKYC GERSQFVVSS
NSSKITVHFH SDHSYTDTGF LAEYLSYDSN DPCPGMFMCK TGRCIRKELR CDGWADCPDY
SDERYCRCNA THQFTCKNQF CKPLFWVCDS VNDCGDGSDE EGCSCPAGSF KCSNGKCLPQ
SQKCNGKDNC GDGSDEASCD SVNVVSCTKY TYRCQNGLCL SKGNPECDGK TDCSDGSDEK
NCDCGLRSFT KQARVVGGTN ADEGEWPWQV SLHALGQGHL CGASLISPDW LVSAAHCFQD
DKNFKYSDYT MWTAFLGLLD QSKRSASGVQ ELKLKRIITH PSFNDFTFDY DIALLELEKS
VEYSTVVRPI CLPDATHVFP AGKAIWVTGW GHTKEGGTGA LILQKGEIRV INQTTCEDLM
PQQITPRMMC VGFLSGGVDS CQGDSGGPLS SAEKDGRMFQ AGVVSWGEGC AQRNKPGVYT
RLPVVRDWIK EHTGV
