ID W5UEB9_ICTPU Unreviewed; 840 AA.
AC W5UEB9; A0A2D0QTU2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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|EMBL:AHH38057.1};
GN Synonyms=st14a {ECO:0000313|RefSeq:XP_017321848.3};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH38057.1};
RN [1] {ECO:0000313|EMBL:AHH38057.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH38057.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_017321848.3}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017321848.3};
RG RefSeq;
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 -!- 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 EMBL; JT407635; AHH38057.1; -; mRNA.
DR RefSeq; XP_017321848.1; XM_017466359.1.
DR RefSeq; XP_017321848.3; XM_017466359.3.
DR STRING; 7998.ENSIPUP00000034780; -.
DR GeneID; 108264634; -.
DR KEGG; ipu:108264634; -.
DR CTD; 678603; -.
DR OrthoDB; 5394933at2759; -.
DR Proteomes; UP000221080; Chromosome 4.
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; 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 2: Evidence at transcript level;
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, ECO:0000313|RefSeq:XP_017321848.3};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..190
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 218..322
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 332..436
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 602..839
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 643
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 696
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 790
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT DISULFID 448..466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 460..475
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 477..489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 484..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 496..511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 514..526
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 521..539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 533..548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 554..566
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 574..589
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 840 AA; 93462 MW; 5EA462DB5618BCE1 CRC64;
MDPMDAGMRY TPKSSDKDWD QAVTFLPATD SKKLEKKKRP GKTGAIIGIV IFAAVVALMT
GLLVWHFHFR KDTKVKKMYA GSMNITNQDF KDAYENPNST EFQALANQVA AQLRELYSRI
PQLSKYYVDS SVQAFSEGSV IAYYLSEFHV PLSQEDAVDN TMKTMDEMIK HKERRLKDST
GNLMFNRIDT SALDSRMFSK PSYYKYAVHT RPNDVIDIMS PGFPNYPYPQ NMLAQWQLRA
DPGHIIKLEF TTFNLEENCR NDFMKVYDSL VAIESRLMAE KCGHYSPNNP LGFISSGNVM
LVTMVTNDIG DYPGFRAQVS QVVGGSTRAM SCGGTLTGTS GTFTSPNYPK YYPTFIRCEW
KIQVPSNMHV KLVFSKFMMS LGGACLTDYV QVNDEKLCGE LPSSTMRTSN SNQMIVVFHS
DASYVDRGFN ATFMAFEPSN PCPDKFLCNN KRCVSSALRC DGWNDCGDSS DERNCHCNST
MISCRNGLCK PMFWKCDGID DCGDKTDEMN CAACKTGEFV CGNGVCISEK QRCDGKNDCG
DKSDEADCER SSVCLETNFK CRNNQCISKQ NPECDGEKDC TDGSDEDKCD VCGMRPFKSS
RIVGGQDSME GEWPWQVSLH IKNSVHVCGA SIISDSWLVT AAHCVQDEPK IRLSQPSSWE
VYLGLHTQKQ TDKAEKRYLK RIIAHPSYNE YTFDYDIALM ELDKAVTFRD TIRPICLPSS
SYIFPVGKSV WITGWGATRE GGSGATVLQK AEVRIINSTV CDTLMNGQIT SRMTCAGVLA
GGVDACQGDS GGPMSSSNAV GRMFLAGVVS WGDGCARRNK PGIYTTVPKF RAWIKEQTGV
//
