CBPZ1_PLAF7
ID CBPZ1_PLAF7 Reviewed; 1620 AA.
AC Q8I2A6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Putative zinc carboxypeptidase;
DE EC=3.4.17.-;
GN ORFNames=PF3D7_0103400, PFA0170c;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|EMBL:CAD48994.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP SYNTHESIS OF 497-559, DEVELOPMENTAL STAGE, AND POSSIBLE CANDIDATE MALARIA
RP EPITOPE.
RX PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT "Rapid identification of malaria vaccine candidates based on alpha-helical
RT coiled coil protein motif.";
RL PLoS ONE 2:E645-E645(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual cell-cycle on the
CC cell surface of the host erythrocytes. {ECO:0000269|PubMed:17653272}.
CC -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC determined by epitope response in sera. {ECO:0000269|PubMed:17653272}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255}.
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DR EMBL; AL844501; CAD48994.2; -; Genomic_DNA.
DR RefSeq; XP_001350966.1; XM_001350930.1.
DR AlphaFoldDB; Q8I2A6; -.
DR STRING; 5833.PFA0170c; -.
DR MEROPS; M14.A35; -.
DR PRIDE; Q8I2A6; -.
DR EnsemblProtists; CAD48994; CAD48994; PF3D7_0103400.
DR GeneID; 813171; -.
DR KEGG; pfa:PF3D7_0103400; -.
DR HOGENOM; CLU_243587_0_0_1; -.
DR InParanoid; Q8I2A6; -.
DR OMA; CNQYNDD; -.
DR Proteomes; UP000001450; Chromosome 1.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0035610; P:protein side chain deglutamylation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Membrane; Merozoite;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..1620
FT /note="Putative zinc carboxypeptidase"
FT /id="PRO_0000356829"
FT TOPO_DOM 1..1367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1368..1388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1389..1620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..559
FT /note="Possible malaria epitope"
FT REGION 1279..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1620
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1109
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 1059
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 1062
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 1155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1620 AA; 191963 MW; 0FFE71CA5A7C9765 CRC64;
MLFKNEDSGN GVYCFTYNNF SDVTISDILN IRNDNKNNDN EDNKQDDEEK NDEDDNKSNL
LLEENEENKR QGDKPFEDLS LFSFKNNEQC YDNIKMQQAI LNSSYEKNVK NIVKIVYHED
CKLLYENTDI HVELPSIVYG RNRNKNNDVV NKCNQYNDDD YTNKCNQYND DDYTNKCNQY
NDDDYTNKCN QYNDNDYTNK CNQYNDNDYT NKCNQYNDVR KITNLKYFIN HNWKNINLIN
EKLFLKNLKE LEEILNYNFL HICKNKCKQY NKKRKNERHF SYHDNFLSHY IIYKKNKFIK
HNKNEHINGN HYDAHESTNT YDEEKTREKH NNKNNNMKYC LNKYPYDNVN APLNLSCPWY
EKKIENIYCL NIPGYKYKYK YICPSMSKMN DEKIKELYIP KGHILFNSKF ESGNLKYVIK
EENDKEVYSL FLNPDIRMNE KKNQWFYFSA SYVPNEYYTN ELYKMKMCNK DINHIGDNMN
VVYNYMNGTG NNINNIVNNL DSTVNYMNST GNNINNIVNN LDSTVNYMNS TGNNINNIVN
NLDSTVNYMN STGNNINNIV NNLDSTVNYM NSTGNYLNRK NNNHLSYTNW SGQRCMNQYL
NDINNDEIDT NLDGNRKYSL DACDKFTVRN VRKLEKPFTV RFKIENMAKP FFLYKYGHSP
LSFSECKYKI ENIQWERNSY DIKYIKNSSC KHYNIKKNSM EYYNYNTYTL EFSYDFTYAY
DTVYFASSYP YTYSYLSEYL CLIRNLLKDH PTINYIEERL CKTSCGFDCP VLCITNYDRM
EEYNKEELKE SVEKKQNIVE ANNTCDEKLV DGMDISSNAI RKEIKKKGYI LTSKKLDKNR
VVNNLFVDMK NGCTRGCASG CTNGCANGYT NGYTNRYTKG CTKGCTNEYS NDNMCKECLD
IKNICYQEEK EKCDIIKYND DKDYSHNCCY EECYNMKREK KKFVCCLSDK CNSFLNEQIK
RRRSIMGWNI LRNRIKCCKN KMYTSNDFMK TFDSLLKKVY VCKGENKKNN GTKIIKRFEE
KYDNNLLFKR KDEKRSLSAS PKKKKKKKKK IIVLTARVHP GETNSSYAIH GFIAFIISNN
IYAHILREKF IFIIIPMLNI DGVILGNNRY CYNGFDLNRQ WSNPIGYIHP TIYSAKLLMK
NISENNKIIF FCDFHSHSRK YNCFIFGNEG SYNYVKNKKM CEVFPEIYSH TLPWFALVDT
VYKADNENKG SARLISGKEF SLDCSYTFEI SLFGIQIRKD FNIMYDEKKD IFYVQNYFEG
YQNGDDNIKG GDNIKGGDNI KGDDNINGDD NIKGGDNIKG DDNIKRDDNF QRDDNFQRDD
NFQRGDNFHR GDNFHRDDIY DKMNKHYINN NYYYDKNSYD FLYFDENLLF MTGVSFGICL
FKFINFLSYH KSSICRRTCE EKEKEHISTE TCGILCAKNN KDDEEKCNES KKQNHDAFKT
GNSLEFDKGE EHLLSDTHRM VNTFLCNSMN KSKNKNKNKK GYNYILNKYG FIKLKSSKKH
IEEVKRIRKL KKKKYMVKEV YELGRKIKQN KYYHNYPFGL YKVNINDVIR ILNKINMDDP
NGKYKGPGFN NSVDMKKKIK NKNESKTEKK SKTENKSKSK SKNKSKSKNK SKRKKVIVIL
