A1345_ARTBC
ID A1345_ARTBC Reviewed; 716 AA.
AC D4AYS6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Probable extracellular serine carboxypeptidase {ECO:0000305};
DE EC=3.4.-.- {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_01345;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; ABSU01000019; EFE31746.1; -; Genomic_DNA.
DR RefSeq; XP_003012386.1; XM_003012340.1.
DR AlphaFoldDB; D4AYS6; -.
DR SMR; D4AYS6; -.
DR ESTHER; triec-f2pwm2; Prolylcarboxypeptidase.
DR PRIDE; D4AYS6; -.
DR EnsemblFungi; EFE31746; EFE31746; ARB_01345.
DR GeneID; 9520035; -.
DR KEGG; abe:ARB_01345; -.
DR eggNOG; KOG2182; Eukaryota.
DR HOGENOM; CLU_023630_0_0_1; -.
DR OMA; DVMLNTT; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008758; Peptidase_S28.
DR Pfam; PF05577; Peptidase_S28; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..716
FT /note="Probable extracellular serine carboxypeptidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434502"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 617..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 716 AA; 79307 MW; 8442BEA364E6421D CRC64;
MVKLTACLLL LVAAVQAKLP VTPISQLRAE SHRNKALVAR SQDVNAAFPA HTIQIPIDHF
PKSSRYEPHT TEKFNLRYWF DASHYKEGGP VIILHGGETS GEGRIPFLQK GILAQLAQAT
NGIGVIMEHR YYGGSLPTPD FSNKSLRFLT TEQALADTAY FSKNIKFPGL EKYNLTAPGT
AHILYGGSYA GGQVAFLRTQ YPDIFWGAIS SSGVTKAIYD YWQYFEPIRQ EAPQDCVHVT
QNFVDIVDNI IINGKNANTT RELKNLFGLG RLRDADFANA LSSGITGWQS TNWDPAISGK
SFYQYCGEIT SDRYLYPVTA QQKASAKRII EAGGHGREAP EILPQLLNFV GWLNKSTLES
CSGQGQTAEE CLNSYDEAFY KQDNADQSWR AWPWQYCNEW GYLQTGSGAP KNIRPVISRL
IDLPYTSNIC KQAFGITKPS NVDLVNKYGA FDIEYDRLAF VDGGSDPWKE AGVHATAARK
RGTSTNKPFI LIPDAVHHWD ENGLYPNETT AELPPQRIKE VQAEEARFVK EWMKVHIYID
HQTFTGIRKN LSLMNDELPA HVLPFLVPPT STKNAVSPSH EQPADPRIAI SSWACAGLSV
VVARICCSPI GYRCPSRDLA AQPSKSKKDR RGQQLSPAAG DPIVCTGLTT RLGFVSFLVF
AFSSFTFIPD IETLKAAVLR SGEVLWSHDA AAECCCVLSV LFAASCTESR KLRLDI
