ID A0A3B4ATZ6_9GOBI Unreviewed; 845 AA.
AC A0A3B4ATZ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000019811.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000019811.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- 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; A0A3B4ATZ6; -.
DR STRING; 409849.ENSPMGP00000019811; -.
DR Ensembl; ENSPMGT00000021111.1; ENSPMGP00000019811.1; ENSPMGG00000016038.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 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; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF10; SERINE PROTEASE 56; 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; 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 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 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..187
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 207..323
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 330..440
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 607..844
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 648
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 702
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 796
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT DISULFID 452..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 464..479
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 481..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 488..506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 500..515
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 518..530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 525..543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 537..552
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 560..572
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 580..595
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 845 AA; 93969 MW; BBDEB5FA44B7A55F CRC64;
MEYMDSGLRY TPRKDAGWET TDQFLPVSDH KKLEKKKGPG KVGAVIGVVI FAAVIALMAG
LLVWHFHFRK DIRVKRMYTG SLKITNQVFE DAYENSTTPE FKALAKQVTM QLKSIYAKVP
QLSKYHVGST VQAFSEGSVV AYYLSEFSVP AGQEAAVDSA MTSINQQVEK ERSSYNRPGN
SLMLDDVVSS ALDARMLSTS FQQFLKYSEH ARTNYIGKIE SPGFPNRPYP PNTFIQWQLR
ADPGYLVQLD FDTLNLEENC KNDFVKIYDS LIAIESRVLE ELCGYYSPSE PMTFLSSGNV
MLVTMATNDR GNYPGFRAQV SQVRRGRTTC GGQLTGQKGS FTSPNFPNYY PPDTLCQWTI
TVPEGKAVKV TFNKFLLGEP GQESSKTCRK DYVDIDGKKV CGEKPMKTVT QTSKSNKMTI
TFYSDKSYVD RGFDAQYEAV DMNDPCPKQF QCRNQRCIKS ELKCDGWNDC GDMSDELQCT
CKAKDISCKN GFCKPPFWKC DGIDDCGDGT DELNCGGCPS GHITCENKKC ISEKHRCDGR
DDCGDGTDEL QCNRDSEVTC TETTYKCKNN KCISKVNPEC DGEKDCEDGS DEENCDCGQI
SFKTSRVVGG QDAGEGEFPW QVSLHVKDYG HVCGASIIHP RWLVTAAHCV QDDGKTRFSQ
PGTWEAYFGL HTQRKIGTMV VKKALKQIIP HPYYNHYTFD NDIALMELDS PLTFSDYIKP
ICLPSPQHVF PISSTVWITG WGATREGGFA ASVLQKAQVR MINHDVCNDL MSGQLTSRML
CAGVLSGGVD ACQGDSGGPL NFPEGSRMFL AGVVSWGDGC ARRNKPGIYT TVTKFRGWIK
EKTGA
//
