ID L8ICF0_9CETA Unreviewed; 753 AA. AC L8ICF0; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 27-MAR-2024, entry version 53. 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 ORFNames=E5288_WYG015359 {ECO:0000313|EMBL:MXQ87883.1}, M91_17303 GN {ECO:0000313|EMBL:ELR53863.1}; OS Bos mutus (wild yak). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR53863.1, ECO:0000313|Proteomes:UP000011080}; RN [1] {ECO:0000313|EMBL:ELR53863.1, ECO:0000313|Proteomes:UP000011080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080}, and YakQH1 RC {ECO:0000313|EMBL:ELR53863.1}; RX PubMed=22751099; DOI=10.1038/ng.2343; RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J., RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y., RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y., RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T., RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R., RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P., RA Wang J., Liu J.; RT "The yak genome and adaptation to life at high altitude."; RL Nat. Genet. 44:946-949(2012). RN [2] {ECO:0000313|EMBL:MXQ87883.1, ECO:0000313|Proteomes:UP000322234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WY2019 {ECO:0000313|EMBL:MXQ87883.1}; RC TISSUE=Blood {ECO:0000313|EMBL:MXQ87883.1}; RA Liu Y.; RT "The sequence and de novo assembly of the wild yak genome."; RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases. 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 EMBL; JH881515; ELR53863.1; -; Genomic_DNA. DR EMBL; VBQZ03000041; MXQ87883.1; -; Genomic_DNA. DR RefSeq; XP_005899361.1; XM_005899299.2. DR AlphaFoldDB; L8ICF0; -. DR STRING; 72004.ENSBMUP00000027991; -. DR MEROPS; S08.072; -. DR Ensembl; ENSBMUT00000032243; ENSBMUP00000027991; ENSBMUG00000020957. DR GeneID; 102266289; -. DR KEGG; bom:102266289; -. DR CTD; 5122; -. DR OrthoDB; 5474719at2759; -. DR Proteomes; UP000011080; Unassembled WGS sequence. DR Proteomes; UP000322234; Unassembled WGS sequence. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0030141; C:secretory granule; IEA:Ensembl. DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030070; P:insulin processing; IEA:Ensembl. DR GO; GO:0043043; P:peptide biosynthetic process; IEA:Ensembl. 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:UP000011080}; 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_5033977106" FT DOMAIN 460..597 FT /note="P/Homo B" FT /evidence="ECO:0000259|PROSITE:PS51829" FT REGION 617..657 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 676..695 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 633..650 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; 83772 MW; 1EC4C7C9420D124C CRC64; MGRRAWTLQC TAFSLFCAWC AMNSVKAKRQ FVNEWAAEIP GGPEAASAIA QELGYDLLGQ IGSLENHYLF KHRNHPRRSR RSALHITKRL SDDDRVIWAE QQYEKERSKR SVLRDSALDL FNDPMWNQQW YLQDTRMTAT LPKLDLHVIP VWQKGITGKG VVITVLDDGL EWNHTDIYAN YDPEASYDFN DNDHDPFPRY DPTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPSTWSS VPEKKECVVK DNDFEPRALK ANGEVIIEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE RDTSPNGFKN WDFMSVHTWG ENPIGTWTLR IADMSGRMQN EGRIVTWKLI LHGTSSQPEH MKQPRVYTSY NTVQNDRRGV EKVVDSGEEQ PTQEGLDENA QASQSPSGSG VGGRRDELAE GAPSEAMLRL LQSAFSKNSP SKQSPKKPPS AKPNIPYENF YEALERLNKP SQLKDSEDSL YNDYVDGFYN TKPYKHRDDR LLQALVDLLR EEN //