SPXS5_DICDI
ID SPXS5_DICDI Reviewed; 927 AA.
AC Q54G02;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=SPX and EXS domain-containing protein 5;
GN ORFNames=DDB_G0290647;
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR EMBL; AAFI02000164; EAL62184.2; -; Genomic_DNA.
DR RefSeq; XP_635615.2; XM_630523.2.
DR AlphaFoldDB; Q54G02; -.
DR STRING; 44689.DDB0266490; -.
DR PaxDb; Q54G02; -.
DR PRIDE; Q54G02; -.
DR EnsemblProtists; EAL62184; EAL62184; DDB_G0290647.
DR GeneID; 8627687; -.
DR KEGG; ddi:DDB_G0290647; -.
DR dictyBase; DDB_G0290647; -.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_315337_0_0_1; -.
DR InParanoid; Q54G02; -.
DR OMA; FRRYYDS; -.
DR PhylomeDB; Q54G02; -.
DR PRO; PR:Q54G02; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IBA:GO_Central.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
DR InterPro; IPR004342; EXS_C.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR033507; Syg1.
DR PANTHER; PTHR10783:SF4; PTHR10783:SF4; 1.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 2.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..927
FT /note="SPX and EXS domain-containing protein 5"
FT /id="PRO_0000330824"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..460
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 717..927
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT REGION 54..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 107040 MW; CB17DDA567AC5D9C CRC64;
MKFGKYLESQ VEANRYVDYK GIRKSLKRFK SEIESLNIHI SELKAYNLNN ATSKINSKQP
SPTTATATTT TIGISSSNGG SNLLRNSIST SKFMNLSQTP LGSSTPMPSD QITAINTSKS
ILESMEQLKE IQDRLVKSLT DEVSKVNDFY MEREKEAQER FDKLKIQVPL YLKSKEKQRR
ENEKELNDHD ELLSYSESYH YSKKKNKLNN NNNNNNNNNN NNNNTTSPPP LSHDQQHLQQ
PEIKRINQHH AVLNLTPIKS TPLSPKQQDG SSKKEVKISL LSSPILEEEE EEEEEEDDNI
HDQDPEVIEM ATVYHYDEDE LEEVLSDNCN DNGASDEFNG SVNNNGAGSG GGGNNNSSSE
LNLTFDIIGS KISKSLKEIS THVVKPTTTF FQPLGDRAKR FMSMGKQKSD EALLKEAFRE
YYHFLVILKN YQVINYTGFV KIIKKSEKNT GLSIGSQVMS FIESQQFRQS KKIERLTSSI
EKIHSELFNN GKIRDARKQL RNSEHVSQQS PTISNFFSGV CAGWTSALLM LIYYFIYTKE
FDDFVRFSSI YNVYSAFGLV LLWAFIFGID CWVWTKSHVH YSFIFELSKN KFNHVKIFQA
VTLLSVMWIT SIGVYMWQSV SGDDFPFPFV PPEYNPLVLF GAYMLILVCP FNIFQLSVRK
WFLNTVFRVL TAPIKSVKFK DFFMGDQLSS LVLMIVQFAQ FVCFYTYDVY RPEHSGGCIR
YARYFNPFIS GLPAYCRLMQ CFRRYYDSYD STTGKGDTVH LRNAVKYSLS IVVVVCSTLD
GFFSGDSGWH SPYRLIWVVA GVSNSMYSYW WDLICDWSIV VRPKGQHWNP FKWTLRKRRM
YQPTFVYYFA IFSNLGFRTT WTFTKSLPQL TNILPSYKLV VVIGIIEILR RGQWNIFRLE
NEHLNNCGKF RVTREIPLPY QIRDNEN
