XPR6_YARLI
ID XPR6_YARLI Reviewed; 976 AA.
AC P42781;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Dibasic-processing endoprotease;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=XPR6; OrderedLocusNames=YALI0F13189g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 32338 / CX-161-1B;
RX PubMed=8203153; DOI=10.1002/yea.320100107;
RA Enderlin C.S., Ogrydziak D.M.;
RT "Cloning, nucleotide sequence and functions of XPR6, which codes for a
RT dibasic processing endoprotease from the yeast Yarrowia lipolytica.";
RL Yeast 10:67-79(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
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DR EMBL; L16238; AAA20573.1; -; Genomic_DNA.
DR EMBL; CR382132; CAG78169.1; -; Genomic_DNA.
DR PIR; S40697; S40697.
DR RefSeq; XP_505362.1; XM_505362.1.
DR AlphaFoldDB; P42781; -.
DR SMR; P42781; -.
DR STRING; 4952.CAG78169; -.
DR PRIDE; P42781; -.
DR EnsemblFungi; CAG78169; CAG78169; YALI0_F13189g.
DR GeneID; 2907885; -.
DR KEGG; yli:YALI0F13189g; -.
DR VEuPathDB; FungiDB:YALI0_F13189g; -.
DR HOGENOM; CLU_002976_2_1_1; -.
DR InParanoid; P42781; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007323; P:peptide pheromone maturation; IEA:EnsemblFungi.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.40.50.200; -; 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 Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 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; Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..976
FT /note="Dibasic-processing endoprotease"
FT /id="PRO_0000027201"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 277..595
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 604..737
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 172..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 528
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 976 AA; 110024 MW; 038C5999E7E8F6F6 CRC64;
MLRKFILGLL LASQAVAQLP HKERDYDSRV YVALSLRDGL DPREFEASVS GLDHGQWTFE
HPVGTIPNTY VFSAPKEYAP IENIRDQDRL EVAGGVLAKR ELRKREKLQK KYGMSEEDVE
KRLVALERLD YDWSERGLGS LEVLSERRIH KRAPVNWTEE EMEYLKEIKR RAEEAQKAQD
DKGDKKEDQK DDKKEGQEAQ KEGDKEDNKG DDKEDGEEDD DDDEDEDDDD ASPAMPVQWK
PVDESMYGGM PDDSLYDVYR KYYPDEVGIK DPSLWKQWYL HNVHKAGHDL NVTGLWLRNV
TGWGVVTAVV DDGLDMNAED IKANYFAEGS WDFNFNKSDP KPSSHDDYHG TRCAGEIAAV
RNNVCGVGVA YDSKVAGIRI LSKEIAEDIE ALAINYEMDK NDIYSCSWGP PDNGQTMARP
GKVVKDAMVN AITNGRQGKG NVFVFASGNG GSRGDNCNFD GYTNSIYSIT VGALDFNDGH
PYYSEACSAN MVVTYSSGSE HYIVGTDINA IDDKSAAPRC QNQHGGTSAA APLAAGVFAL
ALSVRPDLTW RDMQYLALYS AVEINSNDDG WQDTASGQRF HHQFGYGKLD ASKIVELAEG
WNLVNNQTSF HSEVKTVSQK VKYNEPLKSV ITVTRDDLDK VNFKRAEHIT AVLNLEASYR
GHVRVLLKGP RGVVSELAAL RRDDRSKDGY DNWAFMSVAH WADEGEGDWE LTVENTGEQD
QVELVNWQLN VFGEQKDKRE ENKEGESKPE DENKEGEKEG EKKPEDENKE EGNKEDDKGD
QKEDKPEDKP EDKPEDTPED KPEDKPEDAP EDKPSDEKKP EEKPEEKPVD NSDSSSDSSD
SHTSWWPDLS SKKSAWLYGA VLLVGGFIAV IGIYACVTRR NRVRRNRSKD APSASSFEFD
LIPHDDSDDD FVYPEDTHRR SGDNDRLYDP FAEVEDDDDM FRISDEGEDA HDVEPELNRV
SMEADKRDND RQNLLG
