ST14_BOVIN
ID ST14_BOVIN Reviewed; 855 AA.
AC Q0IIH7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Suppressor of tumorigenicity 14 protein homolog;
DE EC=3.4.21.109;
DE AltName: Full=Serine protease 14;
GN Name=ST14; Synonyms=PRSS14;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Degrades extracellular matrix. Proposed to play a role in
CC breast cancer invasion and metastasis. 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:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; BC122638; AAI22639.1; -; mRNA.
DR RefSeq; NP_001070006.1; NM_001076538.1.
DR AlphaFoldDB; Q0IIH7; -.
DR SMR; Q0IIH7; -.
DR STRING; 9913.ENSBTAP00000026272; -.
DR MEROPS; S01.302; -.
DR GeneID; 767617; -.
DR KEGG; bta:767617; -.
DR CTD; 6768; -.
DR InParanoid; Q0IIH7; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000285891"
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..334
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 340..447
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 452..487
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 487..524
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 524..560
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 566..603
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 REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:P56677"
FT CARBOHYD 109
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 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; 94964 MW; DA6E866AAB874F4C CRC64;
MKSERARRGA GGSGDLGAGF KYTSRPENMN GCEEGVEFLP ANNSSKVEKG GPRRWVVLMA
VLAAFLALSL LAGLLAWHFQ DRNVRVQKIF NGYLSVRNEN FLDAYENSNS TEFANLAKKV
KEALKFLYSG IPVLGPYHKT STVTAFSEGS VIAYYWSEFD IPKHLVKEAE QAMAEKRMVT
VPPRARSMSS FVMTSVVAFP SDPRIIQNTQ DNSCSFALHA QGSEPIRFST PGFPDSPYPS
HARCQWTLRG DADSVLSLTF RSFDVATCDE RGSDLVTVYD TLSPVEPRAV VQLCGTYPPS
YNLTFLSSQN VLLITLVTST ERRHPGFEAV FFQLPRMSSC GGYLRAAQGT FNSPYYPGHY
PPNINCTWHI EVPDNKNVKV RFKAFFLQEP NVPVGSCTKD YVEINGEKYC GERPQFVASS
RNNKITVHFH SDQSYTDTGF LAEFLSFDAR DPCPGSFMCN TGRCIRKELR CDGWADCTDY
SDELDCKCNA TYQFTCRDKF CKPLFWVCDS VKDCEDGSDE EGCSCPPNTF KCGNGKCLPQ
SQQCDRKDDC GDGSDEAKCQ DGKAVPCTEH THRCLNGLCV DKSNPQCDGN EDCTDGSDEK
DCDCGRRSFT RQSRVVGGEN SDQGEWPWQV SLHAQGHGHL CGASLISPSW MISAAHCFVD
DRGFRYSEHS VWTAFLGLHD QSKRNAPGVQ ERGLQRIIKH PFFNDFTFDY DIALLQLDRP
VEYSATIRPI CLPAADYTFP TGKAIWVTGW GHTQEAGQGA MILQKGEIRV INQTTCEHLL
PQQITPRMIC VGYLSGGVDA CQGDSGGPLS SPEEDGRMFQ AGVVSWGEGC AQRNKPGVYT
RLPVFRDWIK AQIGV
