PFF1_COCP7
ID PFF1_COCP7 Reviewed; 1012 AA.
AC C5P998;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Vacuolar membrane protease {ECO:0000250|UniProtKB:P38244};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-related family protease 1 {ECO:0000250|UniProtKB:P38244};
GN ORFNames=CPC735_004820;
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000250|UniProtKB:P38244}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P38244};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; ACFW01000030; EER26310.1; -; Genomic_DNA.
DR RefSeq; XP_003068455.1; XM_003068409.1.
DR AlphaFoldDB; C5P998; -.
DR SMR; C5P998; -.
DR EnsemblFungi; EER26310; EER26310; CPC735_004820.
DR GeneID; 9693938; -.
DR KEGG; cpw:CPC735_004820; -.
DR VEuPathDB; FungiDB:CPC735_004820; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Transmembrane; Transmembrane helix; Vacuole; Zinc.
FT CHAIN 1..1012
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411712"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 61..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..432
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 433..453
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 488..508
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..518
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 519..539
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 551..571
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..575
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 576..596
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 711..731
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..743
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 744..764
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 778..798
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 799..1012
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 614..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 359
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1012 AA; 112348 MW; 33E7958205ACB3B7 CRC64;
MRRSTDPRNL LVRRGPLLVD GESAISELDP GFFPTGDAPK MSSTTRRRFN LIAFTPGPVT
VISSLVYLAL LIPLLLVHTI VPSAPKSNPK GVDLSEAWND LQHLTSGFHP YNSHRNDEIH
QWLLQRVGHI LDASRKAHED DAMGSVAPDV FVFDDQQSNL TFSGGGVGNK PITGVYFEGK
NIIVYIRGLE DDKENWWDSP GGKPKGKGGV LVNAHYDSVS TGFGATDDGV GVVSVLQLIK
FFTSPGNLPR KGLVLLLNNG EEDYLNGARA YSQHPLSKYT HTFLNLEGAG AGGRAALFRT
TDIEVTRFYK SSPHPFGSVL AADGFKMGLI RSETDYAVFK GVLGLRGLDV AFIEPRARYH
TDQDDVRHTS IDSVWHMLSA AIATTKGLVS YTGSEFDGRA PGKGMVNSGV GTHGVWFDLF
GSSFAVFRLH TLFAISVTLL VVCPIVLFVI GIILSKMDKM YLFSIHETIP ETKEKVSVRG
LRGLFRYPII LVVSSGILIG LSYLLAKVNP FIVHSSSYAV WSMMLSSWIF MTWFLSCIAD
FFRPSALHRA YTFTWQLLVM WVLLVISTVY VNQHDIAAGY FIVFYFAGTF LATLISYLEL
FALPNKTRYA REQSQYPSRL GSNRSSRILS PSADELPTGG DNNGEIYDGE EEPTESSSLL
GRQRRTTFAN YTRTGRDLAS SESGTYEDHS ETGVFGEEQK WSASLPTWTW VLQFLFVGPV
VIMFIGQLGL FLTSAMNQVG ADGVGLLVVY IAIAVFSVLL LIPLSPFIHR FTYHVPTFLL
LVFIATLIYN LAAFPFSAEN RLKIFFVQEL NLDTGRNQVS LTGVDPYVQD IIRAIPSASK
ENISCDSELD SGRRKCSWPG LAPEVVQDEP TDRWLSFNIS KPSSQETKDT PVLHARLHVS
GKNTRACRVN FERPIRDYSL PGSALDDRMP HTLPQGISEI RLWSRTWENV WTVDVQWDAE
DMDELHGRVV CLWSDANQLG SIPALDELRL FAPPWVAISK LKDGLVEVSR GF
