ID A0A091DEV1_FUKDA Unreviewed; 542 AA.
AC A0A091DEV1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Neuroendocrine convertase 2 {ECO:0000313|EMBL:KFO29033.1};
GN ORFNames=H920_09555 {ECO:0000313|EMBL:KFO29033.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO29033.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO29033.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO29033.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; KN122654; KFO29033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DEV1; -.
DR STRING; 885580.ENSFDAP00000013465; -.
DR MEROPS; S08.073; -.
DR eggNOG; KOG3526; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016486; P:peptide hormone processing; IEA:UniProt.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; 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 PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 365..501
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 288
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 542 AA; 59506 MW; 05B9191C608616A6 CRC64;
MALQQEGFDR KKRGYRDINE IDINMNDPLF TKQWYLINTG QADGTPGLDL NVAEAWELGY
TGKGVTIGIM DDGIDYLHPD LASNYNAEAS YDFSSNDPYP YPRYTDDWFN SHGTRCAGEV
SAAANNNICG VGVAYNSKVA GIRMLDQPFM TDVIEASSIS HMPQLIDIYS ASWGPTDNGK
TVDGPRELTL QAMADGVNKG RGGKGSIYVW ASGDGGSSDD CNCDGYASSM WTVSINSAIN
DGRTALYDES CSSTLASTFS NGRKRNPEAG VATTDLYGNC TLRHSGTSAA APEAAGVFAL
ALEANMGLTW RDMQHLTVLT SKRNQLHDEV HQWRRNGVGL EFNHLFGYGV LDAGAMVKMA
KDWKTVPERF HCVGGTVQDP EKIPSTGKLV LTLTTAACEG KENFVRYLEH VQAVITVNAT
RRGDLNINMT SPMGTKSILL SRRPRDDDSK VGFDKWPFMT THTWGEDARG TWTLELGFVG
STPQKGVLKE WTLMLHGTQS APYIDQVVRD YQSKLAMSKK QELEEELDEA VERSLKSILG
KN
//