ID I3J8E1_ORENI Unreviewed; 807 AA.
AC I3J8E1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Suppression of tumorigenicity 14 {ECO:0000313|Ensembl:ENSONIP00000005131.2};
GN Name=st14 {ECO:0000313|Ensembl:ENSONIP00000005131.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005131.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000005131.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
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; I3J8E1; -.
DR Ensembl; ENSONIT00000005135.2; ENSONIP00000005131.2; ENSONIG00000004071.2.
DR GeneTree; ENSGT00940000164481; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR Proteomes; UP000005207; Linkage group LG14.
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; 3.
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; 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 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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Serine protease {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 36..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..191
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 182..308
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 317..408
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 569..806
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 420..438
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 432..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 455..473
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 467..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 484..496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 491..509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 503..518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 523..535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 543..558
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 807 AA; 89182 MW; 6B57F148D353F7CC CRC64;
LSFAPLSTQD KDWDINVHLP ASNTKRLEKK KHPGKTGAVI GVVIFAAVVA LMVGILVWHF
HFRKHQRVKR MYSGSMRITN QAFINAYENS STPEFKALAK QVISQLKVVY SKSPQLSKYY
RESTVQAFSE GSVIAYYLSE FNVPVGQERA VDNEMTSVET LVKKMRNSMR TSNELTFENV
VTSGTVKATA SHSVYIKHTL LFVILSSPGF PDSPYPPNTF IQWQLRADPG YVVKLEFGTF
ELEESCENDF IKIYDSLVPI ESLLMEELCG KYLPNKRLSF LSSGNVMLVT MATHDQSFPG
FIAEVSQVQK GNKAIACGEK LIGSKGNFSS PNHPNYYPPK ITCEWLIEVS GQSLKWCVIA
CTFHFFRWCG EKPDGSVTET SSTNNMTVVF YSDESRVDHG FSAQYEAIDV QNPCPDKFRC
RNNNCIKLAL KCDGWNDCGD MSDELECSDS ADIRCRNGFC KPMFWKCDGV NDCGDNTDEM
DCGCASGQIT CKNGNCVSEK LKCDGKDDCG DGTDEQDCLT VSCTDFTYKC KDNKCISKVN
PECDGMTDCG DGSDEENCDC GTRGKSQRIV GGQNAELGEF PWQISLHVKS HGHVCGASLI
SPKWLVTAAH CVQDEGSLKL SQPGSWEVYL GLHEQRKTQD PVQKRNLKQV IPHPNYNKFT
FDNDIALMEL DSPVTYSDFI KPICLPAPQH EFPPGQSVWI TGWGATREGG SAAVVLQKAS
VRIINQAVCN ELMGGQITSR MFCAGVLTGG VDACQGDSGG PLSSLSGSRM FLAGVVSWGD
GCARRNKPGI YTTVTKYRGW IKEKTGV
//
