ID A8X5X3_CAEBR Unreviewed; 1726 AA.
AC A8X5X3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Protein CBR-MRP-1 {ECO:0000313|EMBL:CAP28034.2};
GN Name=mrp-1 {ECO:0000313|WormBase:CBG08145a};
GN Synonyms=Cbr-mrp-1 {ECO:0000313|EMBL:CAP28034.2};
GN ORFNames=CBG08145 {ECO:0000313|WormBase:CBG08145a}, CBG_08145
GN {ECO:0000313|EMBL:CAP28034.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP28034.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP28034.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP28034.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HE600971; CAP28034.2; -; Genomic_DNA.
DR STRING; 6238.A8X5X3; -.
DR WormBase; CBG08145a; CBP44750; WBGene00030001; Cbr-mrp-1.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_2_1; -.
DR InParanoid; A8X5X3; -.
DR OMA; EQESCPD; -.
DR OrthoDB; 3384185at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR CDD; cd18603; ABC_6TM_MRP1_2_3_6_D2_like; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF443; MULTIDRUG-RESISTANCE LIKE PROTEIN 1, ISOFORM I; 1.
DR Pfam; PF00664; ABC_membrane; 3.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 968..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1112..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1161..1192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1204..1225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1269..1291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1297..1323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1393..1415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 306..589
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 621..847
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 978..1452
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1489..1721
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 907..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1726 AA; 192826 MW; 5B54FAA7186956DF CRC64;
MLPLVRELVC GSDNEISALD TKLSYFQLFE GGWRNSTNIP QVSNCGQHTD FSSIPTIFIA
IFSTIVFYQL YESRNAHLRS YSPISLRIIF CCLLLIDLTA TVIYDFSLRF TNSSIYDPIH
LYGDIVQYAG FSLVLVLTIA CRNRGITTSG VITLYWLLVV VCGVPELRYY LSGYNVDPYR
AALYIVSFIF SSLELFLCCF ADTTSNGYIG KNSCPEYTAS FLNQLTFEWF SGLAYLGNKK
SLEKEDLWDL NERDKAKNLI PSFMQNLKPE VERHRKMIKK NPEAIDPKFH PSILFPIFKT
YKFTLLAGGC YKLMFDLLQF VAPELLRQLI SFIEDKNQPM WIGVSIALLM FLSSLIQSMI
LHQYFHEMFR LGMNIRSVLT SAVYSKTLNL SNEAKKGKTT GAIVNLMSVD IQRIQDMTTF
IMLFWSAPLQ ILLSLYFLWK LLGASVLAGF IILILLIPFN SWISVKMRNC QMEQMKYKDE
RIKMMSETLN GMKVLKLYSW EKSMEKMILD VREKEIRVLK KLSYLNAATT LSWACAPFLV
AVLTFGLYVL WDPENNILTP QITFVALALF NILRFPLAVF AMVFSQAVQC AASNTRLREF
FAAEEMAPQS SIAYGGTESA VKIDDGAFAW GPKEEDKSLH NISFDIKRGQ LVAVIGRVGS
GKSSLLHALL GEMNKLSGSV QVNGSVAYVP QQAWIQNLSL RNNILFNKTY DEKLYRKVIE
SCALVQDLES LPAEDRTEIG EKGINLSGGQ KQRVSLARAV YQNSEIVLLD DPLSAVDSHV
GKHIFENVIS SATGCLATKT RILVTHGLTY LKHCDKVIVL KDGTISEMGT YQELMNSNGA
FAEFLEEFLL EESKHRGRSI SFGEDSKEVD EILHDLDQVS PSIRQRIQSQ MSQEIDRVDE
KNAEIVSNGH QRNESAHSPA GKSDEKEALL GPKTKEKTPE PPKQAKTQLI EREAVETGKV
KFEIYMSYFR AIGMLIALVF FLVYVASSVL GVFSNLYLAR WSDDAKRIAL AGNVSARETY
VRLGVYAMLG MGQAISVCMA SVIMALGMVR ASRLLHGGLL HNMMRSPMAF FDVTPLGRIL
NRFGKIVSQD MDVVDERLPD NFGDFLLTFS ELVSCVVFTT YATPVSIFAI AFIAVGCLFI
LDIEAVDQTL PHSIRAMVMT IFNVISTVVV IIWATPWAGI AFFVLGLIYF VVLDVDVIDS
RLPACIMTFV GAIVQAVTIF AVPIYATPGS LLIIVPTLYG YLRLLDVDGV DTEIPRSMAM
FIRTAEQSIG ILAIILWATP LAISVLLPLL VVYIVVLVRY CCLLFCTSGC VSQLLLVVIY
LLLHRFYVST SRQLKRLESA SRSPIYSHFQ ESIQGASSIR AYGVVDKFVK ESQHKVDENL
ATYYPSIVAN RWLAVRLEMV GNLIVLSAAG AAVYFRDSPG LSAGLVGLSV SYALNITQTL
NWAVRMTSEL ETNIVAVERI KEYTITPTEG NNSLELAAPT WPEKGDILIK NFSVRYRPGL
ELVLHEVSAH VAPSEKVGIV GRTGAGKSSL TLALFRIIEA DGGCIEIDGV NIADLQLEQL
RSRLTIVPQD PVLFSGTLRM NLDPFDAFND DQIWEALRNA HLESFVNSLQ HGLSHKISEG
GENLSVGQRQ LICLARALLR KTKVLVLDEA AAAVDVETDS LLQKTIREQF KECTVLTIAH
RLNTVMDSDR LLVLDKGRVA EFDTPKRLLA NPDGIFYSMA KDANVL
//
