ID A0A2Y9DIX8_TRIMA Unreviewed; 753 AA.
AC A0A2Y9DIX8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Neuroendocrine convertase 1 {ECO:0000256|ARBA:ARBA00015312};
DE EC=3.4.21.93 {ECO:0000256|ARBA:ARBA00013234};
DE AltName: Full=Prohormone convertase 1 {ECO:0000256|ARBA:ARBA00031320};
DE AltName: Full=Proprotein convertase 1 {ECO:0000256|ARBA:ARBA00032862};
GN Name=LOC101353481 {ECO:0000313|RefSeq:XP_004375097.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004375097.1};
RN [1] {ECO:0000313|RefSeq:XP_004375097.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in the processing of hormone and other protein
CC precursors at sites comprised of pairs of basic amino acid residues.
CC Substrates include POMC, renin, enkephalin, dynorphin, somatostatin,
CC insulin and AGRP. {ECO:0000256|ARBA:ARBA00002975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of protein hormones, neuropeptides and renin from
CC their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.;
CC EC=3.4.21.93; Evidence={ECO:0000256|ARBA:ARBA00000779};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000256|ARBA:ARBA00004398}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR RefSeq; XP_004375097.1; XM_004375040.1.
DR AlphaFoldDB; A0A2Y9DIX8; -.
DR STRING; 127582.A0A2Y9DIX8; -.
DR GeneID; 101353481; -.
DR KEGG; tmu:101353481; -.
DR InParanoid; A0A2Y9DIX8; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000248480; Unplaced.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 6.10.250.3320; -; 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; IPR022005; Proho_convert.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12177; Proho_convert; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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:UP000248480};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..753
FT /note="Neuroendocrine convertase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015958445"
FT DOMAIN 460..597
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 622..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 753 AA; 83654 MW; C0C6EF731E02EA8C CRC64;
MELRAWTLQG TALALFCALC ALNCVGAKRQ FVNEWAAEIS GGPEAASAIA EELGYDLLGQ
IGSLENHYLF KHKNHPRRSR RSALHITKRL SDDVRVIWAE QQYEKDRSKR TALKDSALNL
FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWQKGITGKG VVITVLDDGL EWNHTDIYAN
YDPEASYDFN DNDHDPFPRY DPTNENKHGT RCAGEIAMQA NNHKCGVGIA YDSKVGGIRM
LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
TDQRITSADL HDDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWSS VPEKKECVVK DNDFEPRALK
ANGEVIIEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE
RDTSPNGFKN WDFMSVHTWG ENPVGTWTLR VTDMSGRTQN EGRIVNWKLI LHGTAPQPEH
MKQPRVYTSY NTVQNDRRGV EKMVHSGEEQ PTPENLNENP LVAKSPSSSS VGNRRDEMAG
GAPSEAMLRL LQSAFSKNSP SKQSPKKSPS AKLNIPYENF YEALEKLNKP SQLRDSEDSL
YNDYVDVFYN TKPYKHRDDR LLQALVDILN EEN
//
