YOP1_PLABA
ID YOP1_PLABA Reviewed; 226 AA.
AC A0A509ADH4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Protein YOP1 homolog {ECO:0000303|PubMed:27484902};
DE Short=PbYOP1 {ECO:0000303|PubMed:27484902};
GN Name=YOP1 {ECO:0000303|PubMed:27484902};
GN ORFNames=PBANKA_0414500 {ECO:0000312|EMBL:VUC54370.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 2-ARG--ASN-38; LEU-45;
RP LEU-49; VAL-52; 171-ALA--VAL-226 AND 187-GLU--VAL-226.
RX PubMed=27484902; DOI=10.1007/s13238-016-0290-5;
RA Sun S., Lv L., Yao Z., Bhanot P., Hu J., Wang Q.;
RT "Identification of endoplasmic reticulum-shaping proteins in Plasmodium
RT parasites.";
RL Protein Cell 7:615-620(2016).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=32432369; DOI=10.1111/mmi.14526;
RA Shi X., Hai L., Govindasamy K., Gao J., Coppens I., Hu J., Wang Q.,
RA Bhanot P.;
RT "A Plasmodium homolog of ER tubule-forming proteins is required for
RT parasite virulence.";
RL Mol. Microbiol. 114:454-467(2020).
CC -!- FUNCTION: Required to generate and maintain the structure of the
CC tubular endoplasmic reticulum network and the digestive (food) vacuole
CC (PubMed:27484902, PubMed:32432369). Induces high curvature in membranes
CC and causes membrane tubule formation (PubMed:27484902).
CC {ECO:0000269|PubMed:27484902, ECO:0000269|PubMed:32432369}.
CC -!- SUBUNIT: May form oligomers. {ECO:0000269|PubMed:27484902}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:32432369}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage (at
CC protein level) (PubMed:32432369). Expressed in sporozoites (at protein
CC level) (PubMed:32432369). Not expressed in host liver 48 hours post-
CC infection (at protein level) (PubMed:32432369).
CC {ECO:0000269|PubMed:32432369}.
CC -!- DOMAIN: The N-terminus is important for protein stability.
CC {ECO:0000269|PubMed:27484902}.
CC -!- DOMAIN: The C-terminus is dispensable for the formation of membrane
CC tubules. {ECO:0000269|PubMed:27484902}.
CC -!- DOMAIN: The short lumenal loops between transmembrane domains 1 and 2
CC and between transmembrane domains 3 and 4 may impart a wedge-like
CC configuration, thus deforming membranes.
CC {ECO:0000250|UniProtKB:Q12402}.
CC -!- DISRUPTION PHENOTYPE: During the asexual blood stage, parasites have a
CC slower growth, a delayed ring-to-trophozoite transition and display
CC abnormal endoplasmic reticulum architecture and an enlarged digestive
CC vacuole (PubMed:32432369). In infected mice, the number of male and
CC female gametes is reduced, resulting in a severe decrease in the number
CC of midgut oocytes and salivary gland sporozoites in the mosquito
CC (PubMed:32432369). Sporozoites have a slight reduction in motility and
CC the invasion of host hepatocytes is slightly delayed (PubMed:32432369).
CC In C57BL/6 mice, parasitemia is reduced and the parasite fails to
CC induce experimental cerebral malaria (ECM) (PubMed:32432369).
CC {ECO:0000269|PubMed:32432369}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000255|RuleBase:RU362006}.
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DR EMBL; LK023119; VUC54370.1; -; Genomic_DNA.
DR RefSeq; XP_673809.1; XM_668717.1.
DR STRING; 5823.A0A509ADH4; -.
DR VEuPathDB; PlasmoDB:PBANKA_0414500; -.
DR OMA; FILVLWM; -.
DR Proteomes; UP000074855; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IDA:UniProtKB.
DR GO; GO:0007033; P:vacuole organization; IMP:UniProtKB.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..226
FT /note="Protein YOP1 homolog"
FT /id="PRO_0000454706"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 93..94
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 114..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 124..140
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 141..143
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 163..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 2..38
FT /note="Missing: Does not affect membrane tubule formation;
FT when associated with 171-A--V-226 DEL or with D-45, D-49,
FT D-52 and 187-E--V-226 DEL."
FT /evidence="ECO:0000269|PubMed:27484902"
FT MUTAGEN 45..52
FT /note="LSGKLEQV->DSGKDEQD: Does not affect membrane tubule
FT formation; when associated with 2-R--N-38 DEL and 187-E--V-
FT 226 DEL."
FT /evidence="ECO:0000269|PubMed:27484902"
FT MUTAGEN 45
FT /note="L->D: Does not affect membrane tubule formation;
FT when associated with D-49, D-52, 2-R--N-38 DEL and 187-E--
FT V-226 DEL."
FT /evidence="ECO:0000269|PubMed:27484902"
FT MUTAGEN 49
FT /note="L->D: Does not affect membrane tubule formation;
FT when associated with D-45, D-52, 2-R--N-38 DEL and 187-E--
FT V-226 DEL."
FT /evidence="ECO:0000269|PubMed:27484902"
FT MUTAGEN 52
FT /note="V->D: Does not affect membrane tubule formation;
FT when associated with D-45, D-49, 2-R--N-38 DEL and 187-E--
FT V-226 DEL."
FT /evidence="ECO:0000269|PubMed:27484902"
FT MUTAGEN 171..226
FT /note="Missing: Does not affect membrane tubule formation;
FT when associated with 2-R--N-38 DEL."
FT /evidence="ECO:0000269|PubMed:27484902"
FT MUTAGEN 187..226
FT /note="Missing: Does not affect membrane tubule formation;
FT when associated with D-45, D-49, D-52 and 2-R--N-38 DEL."
FT /evidence="ECO:0000269|PubMed:27484902"
SQ SEQUENCE 226 AA; 26311 MW; 5F7E10A3B73775E4 CRC64;
MRMSKLYKNK EKENEKPSNE PPIKQDSLKR MSSKFLGNSL NSFDLSGKLE QVDEYLKKYP
FIIEFGYKLG IKPSYIVVFG GSALFISLVL GWGAALICNL VGFAYPAYQS FKAVESQGHA
ETKLWLTYWV VFSLFFFIEY LIDIILFWIP FYYVIKLLFL LYLYMPQVRG AETVYNYIIR
PILLKHEKTI DDTVHKISQT ATNHLNQFTG NIAEKLVQEG VRRRNV
