ID KEX1_METRA Reviewed; 616 AA. AC E9ESM3; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 22-FEB-2023, entry version 41. DE RecName: Full=Pheromone-processing carboxypeptidase KEX1; DE EC=3.4.16.6; DE AltName: Full=Carboxypeptidase D; DE Flags: Precursor; GN Name=KEX1; ORFNames=MAA_02969; OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium OS anisopliae (strain ARSEF 23)). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium. OX NCBI_TaxID=655844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARSEF 23 / ATCC MYA-3075; RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264; RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X., RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S., RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y., RA Wang C.; RT "Genome sequencing and comparative transcriptomics of the model RT entomopathogenic fungi Metarhizium anisopliae and M. acridum."; RL PLoS Genet. 7:E1001264-E1001264(2011). RN [2] RP GENOME REANNOTATION. RC STRAIN=ARSEF 23 / ATCC MYA-3075; RX PubMed=25368161; DOI=10.1073/pnas.1412662111; RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S., RA St Leger R.J., Wang C.; RT "Trajectory and genomic determinants of fungal-pathogen speciation and host RT adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014). CC -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in CC the C-terminal processing of the lysine and arginine residues from CC protein precursors. Promotes cell fusion and is involved in the CC programmed cell death (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential release of a C-terminal arginine or lysine CC residue.; EC=3.4.16.6; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}. 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; ADNJ02000004; EFZ01740.1; -; Genomic_DNA. DR RefSeq; XP_007819158.1; XM_007820967.1. DR AlphaFoldDB; E9ESM3; -. DR SMR; E9ESM3; -. DR ESTHER; metaq-kex1; Carboxypeptidase_S10. DR MEROPS; S10.007; -. DR GlyCosmos; E9ESM3; 6 sites, No reported glycans. DR GeneID; 19257255; -. DR KEGG; maj:MAA_02969; -. DR HOGENOM; CLU_008523_11_0_1; -. DR OrthoDB; 1647009at2759; -. DR Proteomes; UP000002498; Unassembled WGS sequence. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR018202; Ser_caboxypep_ser_AS. DR PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1. DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. PE 3: Inferred from homology; KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase; KW Membrane; Protease; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..616 FT /note="Pheromone-processing carboxypeptidase KEX1" FT /id="PRO_0000411927" FT TOPO_DOM 29..516 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 517..537 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 538..616 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 469..502 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 578..616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 382 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 444 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT CARBOHYD 119 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 200 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 357 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 433 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 441 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 493 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 616 AA; 68961 MW; 7EC426936D200C65 CRC64; MAPRFSWSLA TSWHALAILA LWPASTLAGD KSAADYYVRE LPGLPKNSPP IKMHAGHIEV TPETNGNLFF WHFQNNHIAN RQRTVIWLNG GPGCSSEDGA LMEVGPYRVT KDNALTLNNG TWNEFANLLF VDNPVGTGFS YVDTNSYIHG LNAMATQFIT FLEKFFALFP EYQSDDLYIA GESYAGQHIP YIARAILDRN KSKSRAETWN LGGLLIGNGW ISPQDQSSAY LKFSLERGLI EKGSDNAQQL QQMQRICDKE MSINPGHVDY PECESILNKI LELTRVGSGD QECINMYDVR LRDSAPSCGM NWPPDLKYVG PYLRQPQVIS ALNLDKQRNT GWQECNSMVN ANFRNQNATA SISLLPDILK EVPILLFSGA EDLICNHVGT EELISNLAWN EGKGFEVTPG NWAPRRQWTF EGEVAGFWQE ARNLTYVLFH NASHMVPFDY PRRSRDMLDR FMKVDISSIG GEPSDSRIDG EKGPDTSVGG AKNNTQQHEE ETKQKLKEAQ WLAYQRSGEV VLVIVIIAAS VWGYFVWRQR RKGTAYSALQ SDEAAGQSRT GLAAFHNRQS DRDLEAAAFD ETTVDNIPLQ ESIGRGESKY SIGDDSDEEE GETNKT //