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Database: UniProt
Entry: Q0IIH7
LinkDB: Q0IIH7
Original site: Q0IIH7 
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   08-MAY-2019, entry version 85.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
CC       in breast cancer invasion and metastasis. Exhibits trypsin-like
CC       activity as defined by cleavage of synthetic substrates with Arg
CC       or Lys as the P1 site (By similarity). Involved in the terminal
CC       differentiation of keratinocytes through prostasin (PRSS8)
CC       activation and filaggrin (FLG) processing (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleaves various synthetic substrates with Arg or Lys at
CC         the P1 position and prefers small side-chain amino acids, such
CC         as Ala and 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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; BC122638; AAI22639.1; -; mRNA.
DR   RefSeq; NP_001070006.1; NM_001076538.1.
DR   SMR; Q0IIH7; -.
DR   MEROPS; S01.302; -.
DR   PRIDE; Q0IIH7; -.
DR   GeneID; 767617; -.
DR   KEGG; bta:767617; -.
DR   CTD; 6768; -.
DR   HOGENOM; HOG000136851; -.
DR   InParanoid; Q0IIH7; -.
DR   KO; K08670; -.
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   CDD; cd00041; CUB; 2.
DR   CDD; cd00112; LDLa; 4.
DR   CDD; cd00190; Tryp_SPc; 1.
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; 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   Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Phosphoprotein; Protease; Reference proteome; Repeat; Serine protease;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    855       Suppressor of tumorigenicity 14 protein
FT                                homolog.
FT                                /FTId=PRO_0000285891.
FT   TOPO_DOM      1     55       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     56     76       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     77    855       Extracellular. {ECO:0000255}.
FT   DOMAIN       86    203       SEA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00188}.
FT   DOMAIN      214    334       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      340    447       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      452    487       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      487    524       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      524    560       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      566    603       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      615    854       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    656    656       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    711    711       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    805    805       Charge relay system. {ECO:0000250}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P56677}.
FT   CARBOHYD    109    109       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    302    302       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    365    365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    489    489       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    772    772       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    214    244       {ECO:0000250}.
FT   DISULFID    340    366       {ECO:0000250}.
FT   DISULFID    397    410       {ECO:0000250}.
FT   DISULFID    453    464       {ECO:0000250}.
FT   DISULFID    459    477       {ECO:0000250}.
FT   DISULFID    471    486       {ECO:0000250}.
FT   DISULFID    488    501       {ECO:0000250}.
FT   DISULFID    496    514       {ECO:0000250}.
FT   DISULFID    508    523       {ECO:0000250}.
FT   DISULFID    525    537       {ECO:0000250}.
FT   DISULFID    532    550       {ECO:0000250}.
FT   DISULFID    544    559       {ECO:0000250}.
FT   DISULFID    567    579       {ECO:0000250}.
FT   DISULFID    574    593       {ECO:0000250}.
FT   DISULFID    587    602       {ECO:0000250}.
FT   DISULFID    641    657       {ECO:0000250}.
FT   DISULFID    776    790       {ECO:0000250}.
FT   DISULFID    801    830       {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
//
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