ABCGM_DICDI
ID ABCGM_DICDI Reviewed; 615 AA.
AC Q55DA0;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ABC transporter G family member 22;
DE AltName: Full=ABC transporter ABCG.22;
GN Name=abcG22; ORFNames=DDB_G0270826;
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).
RN [2]
RP INDUCTION.
RX PubMed=17517120; DOI=10.1186/1471-2164-8-123;
RA Na J., Tunggal B., Eichinger L.;
RT "STATc is a key regulator of the transcriptional response to hyperosmotic
RT shock.";
RL BMC Genomics 8:123-123(2007).
RN [3]
RP FUNCTION.
RX PubMed=18164290; DOI=10.1016/j.yexcr.2007.12.002;
RA Nagasaki A., Uyeda T.Q.P.;
RT "Screening of genes involved in cell migration in Dictyostelium.";
RL Exp. Cell Res. 314:1136-1146(2008).
CC -!- FUNCTION: May be involved in cell migration.
CC {ECO:0000269|PubMed:18164290}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By hperosmotic shock provoked by sorbitol.
CC {ECO:0000269|PubMed:17517120}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72763.1; -; Genomic_DNA.
DR RefSeq; XP_646231.1; XM_641139.1.
DR AlphaFoldDB; Q55DA0; -.
DR SMR; Q55DA0; -.
DR PaxDb; Q55DA0; -.
DR EnsemblProtists; EAL72763; EAL72763; DDB_G0270826.
DR GeneID; 8617187; -.
DR KEGG; ddi:DDB_G0270826; -.
DR dictyBase; DDB_G0270826; abcG22.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_8_1; -.
DR InParanoid; Q55DA0; -.
DR OMA; VFSHIGM; -.
DR PhylomeDB; Q55DA0; -.
DR Reactome; R-DDI-189451; Heme biosynthesis.
DR Reactome; R-DDI-189483; Heme degradation.
DR Reactome; R-DDI-917937; Iron uptake and transport.
DR Reactome; R-DDI-9753281; Paracetamol ADME.
DR PRO; PR:Q55DA0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="ABC transporter G family member 22"
FT /id="PRO_0000391405"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 31..279
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 364..610
FT /note="ABC transmembrane type-2"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 615 AA; 68269 MW; 5925F4DC7FC67035 CRC64;
MDQVSIEMSS TPRPTMVKSK SQLSLRRSLT ITFKDLAYSV TVKKKKMQIL KGVSGTVTPG
ELVAVFGPSG SGKTTLLDIL ANRKESGEIS GAVLINGNEI DDDYKRLCSY VVQEDVLLPT
ITVRETLRFY ADLKLPKSWT EKEKHERIEQ ILEQIGLSHR ADAKIGGVLP GGIVLRGLSG
GEKRRVSIGC GLVTSPSIVL LDEPTSGLDT TSAMAVMKTL VELTQQKSVT VICTIHQPRS
EIFKLFTKIM VLAEGRLVYY GNRPVEHFTE IGFPFPDQTN PADYILDAVT TIKEEGRADE
IADRLQSSYL DQANQESSST LTQSQLGIIN ASGKRKINAY NNGLFTQFLV LWKRTGLDFI
RNPSNCLVRF AVAVFVGLLF GACFSGLGMD EKGVQSRSAV LFYLVINMIL QPFASISLFI
SKRTLFNAER ASKLYHTLPY YLALMFFEIL ACIGTAFILG TITYWFADLN PGADKYFFAM
AILTLAHLAG DFFMLIISCI TVQVDTSFAV GAGVATIYQL FAGFFVPINA LPKSFEWLHW
CNFVYYSFEA LMHNEFVGET VNCGQLACPT GRDVLINLGL NNRGKGINLI IVSSFAFAFF
TMVFLCLHYF HREKR
