ID A0A2C6KY56_9APIC Unreviewed; 779 AA.
AC A0A2C6KY56;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Yip1 domain-containing protein {ECO:0000313|EMBL:PHJ20905.1};
GN ORFNames=CSUI_005259 {ECO:0000313|EMBL:PHJ20905.1};
OS Cystoisospora suis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Cystoisospora.
OX NCBI_TaxID=483139 {ECO:0000313|EMBL:PHJ20905.1, ECO:0000313|Proteomes:UP000221165};
RN [1] {ECO:0000313|EMBL:PHJ20905.1, ECO:0000313|Proteomes:UP000221165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wien I {ECO:0000313|EMBL:PHJ20905.1,
RC ECO:0000313|Proteomes:UP000221165};
RX PubMed=28161402; DOI=10.1016/j.ijpara.2016.11.007;
RA Palmieri N., Shrestha A., Ruttkowski B., Beck T., Vogl C., Tomley F.,
RA Blake D.P., Joachim A.;
RT "The genome of the protozoan parasite Cystoisospora suis and a reverse
RT vaccinology approach to identify vaccine candidates.";
RL Int. J. Parasitol. 47:189-202(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the YIP1 family.
CC {ECO:0000256|ARBA:ARBA00010596}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHJ20905.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MIGC01002545; PHJ20905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6KY56; -.
DR VEuPathDB; ToxoDB:CSUI_005259; -.
DR OrthoDB; 8905at2759; -.
DR Proteomes; UP000221165; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR006977; Yip1_dom.
DR InterPro; IPR039765; Yip5/YIPF1/YIPF2.
DR PANTHER; PTHR12822:SF2; PROTEIN YIPF; 1.
DR PANTHER; PTHR12822; UNCHARACTERIZED; 1.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF04893; Yip1; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000221165};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..38
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 58..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 83221 MW; 17712F7A565B56B4 CRC64;
MATHASLPSN WYEYLDPRGV PYYHNPILNI TQWERPSAPS PGSLNSTHLQ DRGLALSYKE
SNNGRSRDEE RHTRGMVSLG EGDGSLSFLS TSTTSTTPTT SNGTVATGNT RSSISQPPHE
GLPAVTLDLS KDRGSLGGGG QKLSSTRGRG GGVGLDSFSY RNDSLSDSVS SPYSNNRDGA
AVDQRHSNPF ISKNLSGAME ERGKKGWLGA PSSYTDAAGP REAESGRSRG GWSNTILMKF
FPVCHSCFEE TYGTLERLFD VTTEDMLLRL KLVLFPWKSS GESALSGSSV VSRGSGEEGG
GRSRQRRGRD KGNEEECLSY HTSTNADDTS SAGIGEKSGS CFLEKPDLYG PFWTATTLVI
LFFACSNLPF LLFPSSSFTK AKGGGIVTLT IQGPDVRRLS QIAFSVYGCS LLPPLFCWLG
LLWYKHNSSS AATGDEEEGG SAAGLGGDQG RPAFPKLEQL LCLQGYSLVP FCVAGLILLF
LQGLQSGGGG VYFAVSVLRW GVSGVSAASA IFFLYVQLKQ LLAGQEKRVR LVSSAVLIGA
VVVLLAVLLH AVSVGQRIPE KASISKSSAI EGDRGDFSHS PAVVGEFGGE EEKLNHGDDH
LSAKMQLTDT EEQGGHHSRS SAGEDEQILS VDGREGIAEI TASGHHHDDD NNEAADVHEE
GSASSRHSPL TAPESSNQEN QEHRIQGERK EEGMNSETKP TEDSVKQGGS TASPGQVKKE
DEDEEGKDHG RREGGKVRKE EGSSEEDGRR KEEGRESVHA GVPSAGQKPS KEVDGEPSR
//