YIPF1_DICDI
ID YIPF1_DICDI Reviewed; 347 AA.
AC Q54TS4; B0G137;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Protein YIPF1 homolog;
GN Name=yipf1; ORFNames=DDB_G0281587;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9Y548}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Y548}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q9Y548}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9Y548}. Note=Mainly localizes within
CC medial-/trans-Golgi and trans-Golgi network (TGN), while less so within
CC cis-Golgi. {ECO:0000250|UniProtKB:Q9Y548}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q54TS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q54TS4-2; Sequence=VSP_033033;
CC -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}.
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DR EMBL; AAFI02000042; EAL66555.1; -; Genomic_DNA.
DR EMBL; AAFI02000042; EDR41071.1; -; Genomic_DNA.
DR RefSeq; XP_001732999.1; XM_001732947.1.
DR RefSeq; XP_640517.1; XM_635425.1.
DR AlphaFoldDB; Q54TS4; -.
DR STRING; 44689.DDB0238114; -.
DR PaxDb; Q54TS4; -.
DR EnsemblProtists; EAL66555; EAL66555; DDB_G0281587.
DR EnsemblProtists; EDR41071; EDR41071; DDB_G0281587.
DR GeneID; 8623127; -.
DR KEGG; ddi:DDB_G0281587; -.
DR dictyBase; DDB_G0281587; yipf1.
DR eggNOG; KOG3114; Eukaryota.
DR InParanoid; Q54TS4; -.
DR OMA; HYNFHLV; -.
DR PhylomeDB; Q54TS4; -.
DR PRO; PR:Q54TS4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome 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 InterPro; IPR006977; Yip1_dom.
DR InterPro; IPR039765; Yip5/YIPF1/YIPF2.
DR PANTHER; PTHR12822; PTHR12822; 1.
DR Pfam; PF04893; Yip1; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Endosome; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Protein YIPF1 homolog"
FT /id="PRO_0000330342"
FT TOPO_DOM 1..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y548"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..207
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..255
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..347
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9Y548"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..68
FT /note="MSNYNNKHHDDGNPFYNEPINTSPTQQQQQQQQNLFPNTNIDYNDYTQNRGQ
FT QQQQQPAYQPDLQFQS -> MSTG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_033033"
SQ SEQUENCE 347 AA; 39662 MW; D03D79A1ABCF01EA CRC64;
MSNYNNKHHD DGNPFYNEPI NTSPTQQQQQ QQQNLFPNTN IDYNDYTQNR GQQQQQQPAY
QPDLQFQSFS HDVDVNSNTS PNNNNNNNSN NNNSNKIGGN SSNNKFSDNV PLNTNEDGTE
KKYSFYEVPY YRFLFNVDTK EVGLRLIRSM LPIKFSFFNL IRENPDLYGP FWVLTSLVFI
VAVTSNLNEY FHSSDHKSWE VDIQKIVYSA ITIYGYSFVI PLILWGIFKW MNLGLRLLDM
LCIYGYTLFI FVPASILCVI PLQLVQWIIV AIASIVSGLF LVTNIFTPLK EDFTKRGLII
CAVIGALHIG LALVLKLYFF ANSTENFTIS DSSSTPTPTP TNTTKLL
