ID M3ZTQ7_XIPMA Unreviewed; 772 AA. AC M3ZTQ7; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 27-MAR-2024, entry version 65. 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}; OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae; OC Xiphophorus. OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000005600.1, ECO:0000313|Proteomes:UP000002852}; RN [1] {ECO:0000313|Proteomes:UP000002852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852}; RA Walter R., Schartl M., Warren W.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000002852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852}; RX PubMed=23542700; DOI=10.1038/ng.2604; RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A., RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P., RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S., RA Postlethwait J.H., Warren W.C.; RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into RT evolutionary adaptation and several complex traits."; RL Nat. Genet. 45:567-572(2013). RN [3] {ECO:0000313|Ensembl:ENSXMAP00000005600.1} RP IDENTIFICATION. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000005600.1}; RG Ensembl; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_005813881.1; XM_005813824.1. DR AlphaFoldDB; M3ZTQ7; -. DR STRING; 8083.ENSXMAP00000005600; -. DR MEROPS; S08.072; -. DR Ensembl; ENSXMAT00000005606.2; ENSXMAP00000005600.1; ENSXMAG00000005561.2. DR GeneID; 102231210; -. DR KEGG; xma:102231210; -. DR CTD; 5122; -. DR eggNOG; KOG3525; Eukaryota. DR GeneTree; ENSGT00940000157385; -. DR HOGENOM; CLU_002976_4_1_1; -. DR InParanoid; M3ZTQ7; -. DR OMA; VWQKGFT; -. DR OrthoDB; 5474719at2759; -. DR Proteomes; UP000002852; 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: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:UP000002852}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE- KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 27..772 FT /note="Neuroendocrine convertase 1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004047108" FT DOMAIN 467..604 FT /note="P/Homo B" FT /evidence="ECO:0000259|PROSITE:PS51829" FT REGION 633..670 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 685..714 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 174 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 215 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 389 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" SQ SEQUENCE 772 AA; 86091 MW; 5E65DB17037641DA CRC64; MEVRCRPAVM CCVFAVLCSA LSRSQALSYA DRQYLNEWAV EIPGGLSEAE AIAKELDYQL VRQIGALENL FLFKHGSHPR RMRRGAEHIT RQLSEDDRVL WAEQQYEKRR SKRAALRECR DCSVDKLFDD PMWNQQWYLQ DTRSSSSLPK LDLHVIPVWQ KGITGKGVVI TVLDDGLEWN HTDIYANYDP AASYDFNDND PDPFPRYDST NENKHGTRCA GEIAMQADNN KCGVGVAYNS KVGGIRMLDG IVTDAIEASS IGFNPNHVDI YSASWGPNDD GKTVEGPGRL AQKAFEYGIQ QGRNGKGSIF VWASGNGGRQ GDNCDCDGYT DSIYTISISS ASQQGLSPWY AEKCSSTLAT AYSSGDYTDQ RITSSDLHDD CTQTHTGTSA SAPLAAGIFA LALEQNPDLT WRDLQHIVVW TSEFDPLANN PGWKRNGAGL MVNSRFGFGL LNAKALVDLA DPAVWKHMPE KKQCIVRDDA FQPRELKAAG EITIEIPTKA CEGQENAIRS LEHVQVEASI EYTRRGDLHI TLTSPAGTTT VLLAERERDT SSNGFKNWDF MSVHTWGEDP AGTWTLKITD TSGRMENKGR ILNWKLILHG TSEKPEHMKK PRVYIPYNAV QNDRRGVEHM DDMMEEPTQP RPPQKTGAAE ASPSVSEKEP KSPSSGSPRR PSLALLRLLQ TAFKQQATVS QRPGATARPL SARRKQQSRG FLPLPTKLPA HKLYQALDLI NKFSGPGDSL YSDYSDGFYN IKPYKHRNDR LLQALFEMLD DE //