ID A0A3Q4MD14_NEOBR Unreviewed; 805 AA.
AC A0A3Q4MD14;
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=Furin-like {ECO:0000313|Ensembl:ENSNBRP00000007089.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000007089.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000007089.1}
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; A0A3Q4MD14; -.
DR STRING; 32507.ENSNBRP00000007089; -.
DR Ensembl; ENSNBRT00000007291.1; ENSNBRP00000007089.1; ENSNBRG00000005509.1.
DR GeneTree; ENSGT00940000157220; -.
DR OMA; HNEWTAF; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000005509; Expressed in testis and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 1.
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:SF11; FURIN PRECURSOR; 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:UP000261580};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..805
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018574091"
FT TRANSMEM 724..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 439..569
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 161..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 368
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 805 AA; 87238 MW; 2DF64B0E0C66C47D CRC64;
MDAREALLLL WTVFVLLTAE LNWIDGAKVY TNTWAVQING GPGEADRIAR EHGFINHGHV
FGDYYHFRHH AVEKRALSGH KRMHIRLQKE PQVLWTEQQV VKKRKKRDVY EDLTDPDFPK
QWYLSNPTHQ DLNTKAAWAQ GYTGRGVVVT ILDDGIEKDH PDLISNYDPE ASYDVNDGDT
DPQPRYTQRN ENRHGTRCAG EVAGAANNGV CGVGVAYNAK IGGVRMLDGE VTDVVEAQSL
SLNPQHIHIY SASWGPEDDG KSLDGPAKLA KEAFLQGITK GRSGQGSIFV WASGNGGREQ
DSCNCDGYTN SIYTLSISST TQSGNVPWYS EPCSSTLATT FSSGNPGEKQ IVTTDLRQKC
TDSHTGTSAS APLAAGIIAL ALEANVSGLT PHKSQYLSVY SPPPSPLLLK PLLTVSHSYG
YGLLDAGALV ALAQNWTSVG PQHQCVNTML SEPRDIGNKL VFSKSVDACW GRPEHVSSLE
HVQARLTLSY SQRGKLAIHL ISPLGTRSTL LFPRPNDFSS EGFNDWAFMT THSWDEDPQG
EWTLEIENVA PNGRVLSQFT LILWGTGPSI VNPSSPDFPR PSNNSCKTFD AQQICIECSP
GFSLFLQGCV KLCPPGFTSG QQLLNLSLEN WVDLSSVQAC LPCNPACLTC SGTGPADCLS
CPPHSHLVFT SCLHQNQVQR KSPLTGGLQG DGAQPEGASP AAADHDSKGA EESPGLIVAP
STQLPAVVAL LSCAFILAAF VGVFFLLQLR SGGASGRERK ARICYKGIPT VWADEDMIAY
ESESDSEEVD GHSERTAFIK TQSSI
//
