ID A0A1U7QZQ4_MESAU Unreviewed; 855 AA.
AC A0A1U7QZQ4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Suppressor of tumorigenicity 14 protein homolog {ECO:0000256|PIRNR:PIRNR036370};
DE EC=3.4.21.109 {ECO:0000256|PIRNR:PIRNR036370};
DE AltName: Full=Serine protease 14 {ECO:0000256|PIRNR:PIRNR036370};
GN Name=St14 {ECO:0000313|RefSeq:XP_005084503.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005084503.1};
RN [1] {ECO:0000313|RefSeq:XP_005084503.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Exhibits trypsin-like activity as defined by cleavage of
CC synthetic substrates with Arg or Lys as the P1 site.
CC {ECO:0000256|PIRNR:PIRNR036370}.
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 Evidence={ECO:0000256|PIRNR:PIRNR036370};
CC -!- SUBUNIT: Interacts with CDCP1. May interact with TMEFF1.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005084503.1; XM_005084446.3.
DR AlphaFoldDB; A0A1U7QZQ4; -.
DR STRING; 10036.ENSMAUP00000008494; -.
DR GeneID; 101833628; -.
DR KEGG; maua:101833628; -.
DR CTD; 6768; -.
DR eggNOG; KOG3627; Eukaryota.
DR OrthoDB; 5394933at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0060672; P:epithelial cell morphogenesis involved in placental branching; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
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; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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 PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
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; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR036370, ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|PIRNR:PIRNR036370, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PIRNR:PIRNR036370, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Serine protease {ECO:0000256|PIRNR:PIRNR036370,
KW ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..203
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 214..334
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 340..447
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 615..854
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 656
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 711
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 805
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT DISULFID 459..477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 471..486
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 496..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 508..523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 525..537
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 532..550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 544..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 567..579
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 587..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 855 AA; 94545 MW; 6E1CBFBC71A2D41E CRC64;
MGSNRGRKAG GSSKDFGARL KYNSGLENMN GFEEGVEFLP VNNAKKVEKR GPRRCVVLVA
LLVSFLLLSL VAGLLVWHFH YSNVRVQKVF NGHLRVTNEN FLDAYENSNS TEFISLADQV
KEALKLLYSE VPVLGPYHKR SAVTAFSEGS VIAYYWSEFS IPPHLAEEVD RAMAVERVVT
LPPRARALKS FVLTSVVAFP TDPRLLGRTQ DNSCSFALHA HGGEVMRFTT PGFPNSPYPA
HARCQWVLRG DADSVLSLTF RSFDVAPCDE FGSDLVTVYD TLSPMEPHAV VRLCGTYPPS
YNLTFLSSQN VFLVTLITNT DRRHPGFEAT FFQLPKMTSC GGSLSEAQGL FSSPYFPGHY
PPNIDCTWNI KVPNNRNVKV RFKLFYLVDP NVPLGTCPKD YVEINGERYC GEKSQFVVSS
NSSKITVRFH SDHSYTDTGF LAEYLSYDSN DPCPGMFMCN TGRCIQKNLR CDGWADCPDY
SDERFCRCNT THQFMCKNKL CKPLFWVCDS VNDCGDGSDE EGCSCPAETF KCSNGKCLPQ
SQKCNGKDNC GDGSDEASCN SVNVVACTKY TYRCQNGLCL NKGNPECDGK TDCSDGSDEK
NCDCGLRSFT KQARVVGGTN ADEGEWPWQV SLHALGQGHL CGASLISPNW LVSAAHCFMD
DRNFKYSDHT KWTAFLGLLD QSKRSSTGVQ EHKLKRIITH PLFNEITFDY DIALLELEKP
AEYSTVVRPI CLPDPTHVFP AGKAIWVTGW GHTQEGGTGA LILQKGEIRV INQTTCEDLM
PQQITPRMMC VGFLSGGVDS CQGDSGGPLS SVETAGRIFQ AGVVSWGEGC AQRNKPGVYT
RLPAVRDWIK EQTGV
//