KEX1_NEUCR
ID KEX1_NEUCR Reviewed; 659 AA.
AC Q1K722; Q871G2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 70.
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=B7H23.190, NCU04316;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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}.
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DR EMBL; BX294026; CAD71044.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA31726.3; -; Genomic_DNA.
DR RefSeq; XP_960962.3; XM_955869.3.
DR AlphaFoldDB; Q1K722; -.
DR SMR; Q1K722; -.
DR STRING; 5141.EFNCRP00000003856; -.
DR ESTHER; neucr-B7H23.190; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EAA31726; EAA31726; NCU04316.
DR GeneID; 3877103; -.
DR KEGG; ncr:NCU04316; -.
DR VEuPathDB; FungiDB:NCU04316; -.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; Q1K722; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..659
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411930"
FT TOPO_DOM 39..527
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 480..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 659 AA; 72836 MW; 0A063101AF0BDEA3 CRC64;
MAATTTTTNA GRSMASWKRL STLIAAFTLS WTSSFVAAAG SADYFVHDLP GAPDGPLVKM
HAGHIEVTPD NNGNLFFWHF QNKHIANKQR TVIWLNGGPG CSSEDGALME IGPYRLKDEN
TLVYNDGAWN EFANVLFVDN PVGTGFSYVD TNAYIHELTE MAANFVTFLE RWFALFPEYE
HDDLYIAGES YAGQHIPYIA QAILERNKNA GPVNRKWNLS GLLIGNGWVS PKEQYDAYLQ
FAYEKDIVKK GTDLANKLEI QQRICQKEIA VKPDKIDYPE CEAILQDMLQ LTAGGVGASG
KNQCYNMYDV RLKDDYPSCG MAWPPDLKSV TPYLRKKEVI KALNINDNKS TGWTECNGQV
GMNFNPKTKP SITLLPDILS AGVPILLFSG AEDLICNHLG TEALISNMEW NGGKGFELTP
GTWAPRRDWT FEGEPAGFWQ QARNLTYVLF YNSSHMVPFD YPRRTRDMLD RFMGVDISSI
GGQPTDSRLD GEKLPETTVG GAAGNSTSNQ AAEKAKLEMA KWEAYRKSGE LVLVIVIVAA
GVWGWFVWKE RRKTAGQGYM GVATGERHSI SNNPGPRGNL SGGGDRTRGQ GLAGFRNKRS
GRRDVEAQDF DESELDDLHL SKPEDPHADS RYSIGGASDD EEEQKPGKGS SSRQPGGRS