ID A0A3Q0S0B4_AMPCI Unreviewed; 743 AA.
AC A0A3Q0S0B4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 7 {ECO:0000313|Ensembl:ENSACIP00000016167.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000016167.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000016167.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR AlphaFoldDB; A0A3Q0S0B4; -.
DR STRING; 61819.ENSACIP00000016167; -.
DR Ensembl; ENSACIT00000016594.1; ENSACIP00000016167.1; ENSACIG00000012547.1.
DR GeneTree; ENSGT00940000157676; -.
DR OMA; NGRMPFY; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR PANTHER; PTHR42884:SF28; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 7; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 652..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 476..610
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 190..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 402
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 743 AA; 81486 MW; C05F476D23359A83 CRC64;
MAKLYLPTFL LLIFLSSVVL LVLALLPSVT PSFPLASSSH PSLWSSPSCG PGQSWAVRLI
CSCHQYSLWS QVAEQAGLHN HGQIGQLEGH YLLCSSKPGA GSVGRIKRKA VRPEDILAGH
PHVMWYSQER VLSRSKRLMA FNDPNYPKQW HLHNDINKGM DINVTGVWER NITGQGVTVV
VVDDGVEHTH QDIQPNYSPE GSYDLNSNDP DPMPHPDVHS DNHHGTRCAG EIAAVPNNSF
CAVGVAYGSK VAGIRVLDGP LTDSLEAIAF NKHYQINDIY SCSWGPDDDG HTVDGPHPLG
KAALQHGVIA GRRGFGSIFV VASGNGGQYN DNCNYDGYAN SIYTITIGAV DEKGKMPFYA
EECASMLAVT FSSGRGSLRS IVTSDWSMQR GTGCTEGHTG TSAAAPLAAG MVALMLQVRP
CLSWRDVQHI ITFTATKCDN SADWKVNGAG FHHSHQHGFG LLNAWRLVNA AKVWESVPFL
LSYQSSVIKE EAILTYPHEL ILTWEVSAAD LRQSGMETLE HVAVTVTVAH PCRGNVEFVL
VCPSGMTSVI GARRAIDRDN AGYQDWTFST VRCWGERAKG LYTLKISDHS KFLKLTLYGS
SMTFSEVKER QRLVEEAMSG KYLDSRYSLP CPPGLDLPPE ITKPFTSNNL KFMLLLGCFA
LFWSLYYTLE VMMAHLDFRG LLCMPRKRGG HRGRRGRQGK GVEEALIGDE EGEEEEQDSG
VELQAVLDSN VKEPLPSGER LAT
//
