ID A0A2D0PNN3_ICTPU Unreviewed; 892 AA.
AC A0A2D0PNN3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Suppressor of tumorigenicity 14 protein homolog isoform X2 {ECO:0000313|RefSeq:XP_017308203.1};
GN Name=LOC108256139 {ECO:0000313|RefSeq:XP_017308203.1};
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|RefSeq:XP_017308203.1};
RN [1] {ECO:0000313|RefSeq:XP_017308203.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017308203.1};
RG RefSeq;
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 RefSeq; XP_017308203.1; XM_017452714.3.
DR AlphaFoldDB; A0A2D0PNN3; -.
DR GeneID; 108256139; -.
DR KEGG; ipu:108256139; -.
DR OrthoDB; 4167609at2759; -.
DR Proteomes; UP000221080; Chromosome 23.
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; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
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; 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; 1.
DR Pfam; PF00057; Ldl_recept_a; 3.
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; 3.
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; 3.
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 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 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..225
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 258..374
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 379..487
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 651..889
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 35..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 499..517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 511..526
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 570..588
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 582..597
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 604..616
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 624..639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 892 AA; 98291 MW; 7E28BBB165D9B50A CRC64;
MRTFPKNRSC DVYSVSGLGH CGTADSAVQD IKVKEPVQAP SSSSSEIQAG SDIKRPGDRK
ATFRAWRKWA LGAAPLIPLS TAVALTLHFF ASSPSSTVFF LGGSVEFSNL SFSPELADPS
STQFDLQSQA LSPYFSELYE SSPWRPYYRR SGIVAFSEGV NGLNVFFWSK FSAPSATIAE
KLQRSKPAWL QRQLPGTNKV LHSRLEEQYY LAKDEDTLRL LGLNLDSEDD DDDDDMSDKI
KNPNNLQSGK WQLGLQAMSF DLYAKYGNNR TLSLVSPKKP YYQWRLRVPS GHVVRLDVVT
LQGATPGSCS ANKLSAYDFL LPLQNKIIAR WCGLPVTGSS PVMKLTSSGN VMLVTFSFSR
QRHGAIFKAY FQAIPKAECG GFLSAWNGTV VSPYYPAYYP PNVDCNWKIR APLPGYLLSI
TIVMLDIQDS PTTSSCEKDW LEIGGVKLCN PIGDSSRKRI YSSPVLLHFH SDESLTHKGF
YLVYRAFSPE STCPRQFRCG DGRCIPLRKV CDGERDCVDG RDEAKCSMCK PGEVYCGSGQ
CRPHGSQCNL QACGDSSEET NCAGKCYHMC SNKICLPKSS VCDGVLDCRD RSDELNCTRA
YKGCLPTSYK CANGKCIAKV NPECDGIKDC KDGSDEIRCG CGTRPRKRAK IVGGTDAQAG
SWPWQVSLQI ERYGHVCGAS LVSSRWLLSA AHCFQDSDAI KYSDARAWRA YMGMRVMNSA
SNAAATRQIR RIVQHAQYDQ FTSDYDIALL ELSAPVFFND LVQPVCVPAP SHAFTSGTNC
FVTGWGVLTE EGELATLLQE ATVSIINHKT CNKMYDDAVT PRMICAGSIQ GGVDACQGDS
GGPLVCLERG RRWFLAGIVS WGEGCARQNR PGVYTQVIKF TDWIHQQTKG QV
//
