ID G3T345_LOXAF Unreviewed; 852 AA.
AC G3T345;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
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|Ensembl:ENSLAFP00000007640.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007640.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000007640.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007640.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000007640.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007640.3};
RG Ensembl;
RL Submitted (NOV-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}.
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DR AlphaFoldDB; G3T345; -.
DR STRING; 9785.ENSLAFP00000007640; -.
DR MEROPS; S01.302; -.
DR Ensembl; ENSLAFT00000009113.3; ENSLAFP00000007640.3; ENSLAFG00000009113.3.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155418; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR InParanoid; G3T345; -.
DR OMA; PTKWTAF; -.
DR TreeFam; TF330647; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; 1.
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:UP000007646};
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 53..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..200
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 211..331
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 337..444
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 612..851
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 653
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 708
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 802
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT DISULFID 456..474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 468..483
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 493..511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 505..520
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 522..534
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 529..547
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 541..556
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 564..576
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 584..599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 852 AA; 94720 MW; 00290EF726479D4E CRC64;
KGHNFPQSPG WESQDHGLKG HTQKENMNGF EEGVEFLPVN NAKKVEKPGR RCWLVLAAVV
TGFFLLSLVG VLVWHFQYRD VRVQKVFNGH LRIKNENFVD AYENSNSTEF AHLANKVKEA
LKLLYSGIPA LGPYHKDSAV TAFSEGSVIA YYWSEFSVPQ HLVEEAERAM AEEHVVTLPP
RSRALQSMVL TSVVAFPTDP RTVQKTQDNS CSFALHARGR EPTRFATPGF PDSPYPERAH
CQWALRGDAN LVLSLTFRSF DLAPCDQRGS DLVTVYDSLS PIEPSAVVQL CGTYPPSYNL
TFLSSQNVFL VTLITNTERR HPGFEATFFQ LPKMSSCGGY LRQAQGTFSS PYYPGHYPPN
IDCTWNIEVP NKQYVKVRFK LFYLVEPNVS PVTCSKDYVE VNGEKHCGEK SQFVVTSNSS
KMTVRFHSDQ SYTDTGFLAE YLSYDSRDPC PGMFTCNTGR CIRKALRCDG WADCTDHSDE
LNCVCNATHQ FTCKNKFCKP LFWVCDSVND CGDNSDEQGC SCPAQTFRCN NGKCLPLSQQ
CDGTDHCGDG SDEATCDKVS TVTCTEHTYR CHNGLCVSKG NPECDGKEDC SDGSDEKDCD
CGQRSFSKQS RVVGGQNADE GEWPWQVSLH ALGQGHVCGA SLISPTWLVS AAHCHVDDKG
FRYSDPTLWT AFLGLHDQSK RRAPGVQEHK LKRIIRHPNF NDYTYDYDLA LLELEQPAEY
SSLVRPICLP DATHVFPAGK AIWVTGWGHT QEGGSAAVIL QKGEIRVINQ TTCEKLLPQQ
LTARMMCVGY LSGGVDSCQG DSGGPLSSVE ADGRIFQAGV VSWGEGCARR DKPGVYTRLS
MFRDWIKEQT GV
//
