ID A0A3B4GB79_9CICH Unreviewed; 812 AA.
AC A0A3B4GB79;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Furin {ECO:0000313|Ensembl:ENSPNYP00000020165.1, ECO:0000313|RefSeq:XP_005741738.1, ECO:0000313|RefSeq:XP_005741739.1};
GN Name=furin {ECO:0000313|RefSeq:XP_005741738.1,
GN ECO:0000313|RefSeq:XP_005741739.1, ECO:0000313|RefSeq:XP_005741740.1,
GN ECO:0000313|RefSeq:XP_005741741.1, ECO:0000313|RefSeq:XP_005741742.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000020165.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000020165.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005741738.1, ECO:0000313|RefSeq:XP_005741739.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_005741738.1; XM_005741681.2.
DR RefSeq; XP_005741739.1; XM_005741682.1.
DR RefSeq; XP_005741740.1; XM_005741683.1.
DR RefSeq; XP_005741741.1; XM_005741684.2.
DR RefSeq; XP_005741742.1; XM_005741685.2.
DR AlphaFoldDB; A0A3B4GB79; -.
DR STRING; 303518.ENSPNYP00000020165; -.
DR Ensembl; ENSPNYT00000020661.1; ENSPNYP00000020165.1; ENSPNYG00000015245.1.
DR GeneID; 102213582; -.
DR CTD; 566557; -.
DR GeneTree; ENSGT00940000157220; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0060536; P:cartilage morphogenesis; IEA:Ensembl.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IEA:Ensembl.
DR GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0033334; P:fin morphogenesis; IEA:Ensembl.
DR GO; GO:0003146; P:heart jogging; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd00064; FU; 2.
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; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_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:SF31; FURIN (PAIRED BASIC AMINO ACID CLEAVING ENZYME) A; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 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 SMART; SM00261; FU; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 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}; Reference proteome {ECO:0000313|Proteomes:UP000695023};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..812
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041087895"
FT TRANSMEM 719..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 453..585
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 377
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 812 AA; 88226 MW; 9CF9E3AC79FA0BE5 CRC64;
MATGHPSPSV GPRFRLLELL LVPLLVLLVC GPAQGQKVYT NTWAVHVPGG QEEADQIASK
HGFINYGHVF GDYYHFRHRT VVKRSLSDHR GTHVRLLNDP KVTWAEQQVV KQRKKRDVFE
EPLDPKFRDQ WYLYNSNRHD LNAKVAWQLG YTGKGVVVSI LDDGIEKNHP DLMQNYDPDA
SYDVNDGDPD PQPRYTQLND NRHGTRCAGE VAAVASNGIC GVGVAYNAKI GGVRMLDGEV
TDMVEAQSLS LNPQHIDVYS ASWGPEDDGK TVDGPAKLAK EAFMRGVTEG RGGLGSIFVW
ASGNGGREKD SCNCDGYTNS IYTLSISSST QNGNVPWYSE ACSSTLATTY SSGNLNEKQI
VTTDLKSKCT DSHTGTSASA PLAAGIIALA LEANKNLTWR DMQHLVVRTS QPAHLLTNDW
RTNGVGRKVS HSYGYGLLDA GGIVSMAKTW TNVGPQRKCV ITMVSEPRNI GSHLYINKSV
DGCMGTDSHV TSLEHVQARL TLSYNRRGNL AIHLISPAGT RSTLLHPRPH DYSSEGFNDW
AFMTTHSWDE DPTGAWMLEI ENVAGASDYG TLTQFILVLY GTGSTTSSSS EKSQPGNDSC
KTLDLRQICI ECNAGYYLFQ QGCVKECPAG FSVGSQPLNY TVGNFMEPAS VPACLPCPQP
CLTCSSLSPR SCLSCPPHSS LDPNSGTCLH LNQYMRESPD SFMVGPGNQR SQLESGSRLP
ITIAVLSCMA IIATFAGIFL MLQLRSGALI KLPSLEAGSG LGGTFSLGGN RVVSYRGIPT
VWGEEGVNTD SENEEFDVQN ERTAFIKTQS AL
//