ID A0A3Q0SNB1_AMPCI Unreviewed; 1291 AA.
AC A0A3Q0SNB1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ATP-binding cassette, sub-family C (CFTR/MRP), member 4 {ECO:0000313|Ensembl:ENSACIP00000024691.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000024691.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000024691.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR STRING; 61819.ENSACIP00000024691; -.
DR Ensembl; ENSACIT00000025338.1; ENSACIP00000024691.1; ENSACIG00000018894.1.
DR GeneTree; ENSGT00940000153931; -.
DR OMA; MGYAKPL; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016020; C: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 CDD; cd18593; ABC_6TM_MRP4_D1_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; 2.
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; IPR030240; ABCC4_TMD1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF357; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 4; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
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 Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1291
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018554146"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 701..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 852..877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..361
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 412..635
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 711..1004
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1040..1273
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 633..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 144290 MW; A0CEE9DA991A25EB CRC64;
MELTRTGGRH NPLATAGFCS RLFLCWLTPL LQLGKKQSLE ENDMYSILQE DKSETLGGEL
QRFWDREVRH ATKELQKPKL SRVLIKCYGK SYAVAGIFAF FLEAIKVIQP LLLGKIILFF
ENYHHDDQRS LRMAYVYAGA ISISAFGLTI FQHLYYYHVL RTGMQIRVAV CHMIYRKALG
LSAESMGKTT TGQIVNLLSN DVNRFDEITL NLHYLWVGPL QAVVIIVFLW YEIGPSCLAG
VAAIALMMPI QTWFGKLFGI FRSKTAVLTD SRIRIMNEVV SGIRIIKMYA WEKPFSALVT
EVRKKEIHQI LKSSYLRGLN MASFFASSKI TVFVTFTVYS LLGNTITASS VFITASLYGT
IKLTVTLFFP LAIEKLSETV VSIRRIKNFL LLEELERKNV ALPLEGKKEN SIEIEKLTCY
WDKSLDAAAL QNVSXTAKSH QLLTVIGPVG AGKSSLLSAI LGELPHDTGT IKVRGQLTYA
AQQPWVFPGT IRSNILFGRQ LNPKKYERVL RACALKKDLE LFPDGDLTLI GDRGATLSGG
QXARVNLARA VYQDADIYLL DDPLSAVDAE VGKHLFEHCI CGLLKNKCRI LVTHQLQHLK
AADQILVLKE GHIMVQGTYS ELQSSGLDMV SLLRSDEEPR SADPEKLSSH SQRTNRSHDS
HCSSSSLLPP ESSCTDQLPV EGVQTITEET RAEGNVSSHV YLKYFTAGCN LPVLMVILLL
SIIAEVSPNP SKEFSNSTVL TVVSTENGIN VTGSHREINL TFYLSIYSGL TAAAVVFGFV
RSLVIFHGLV RSAQTLHNSM FSAVLRTPVS FFDINPIGRI LNRFSKDVSQ MDSMLPMTFV
DFYQLFWQNA GVIAVAASVI PLILIPVVPL LLFFLYLRSF YLSTSRDIKR LESTTRSPVF
SHLSLSLQGL STIRAFKAEE RLKKTFDTHQ DLHTEAWFLF LMTSRWFALR LDSICSMFIT
LTAFGCILLR DGLEAGAVGL VLTYAVTLIG NFQWTVRQSA EVENMMTSVE RVVEYTELKS
EAPLETQQRP PPDWPSQGMV TFDRVNFFYN TDGPPVLKDI SATFQPQEKV GIVGRTGAGK
SSLVSALFRL AEPRGKICID GVVTSEIGLH DLRQKMTIIP QDPVLFTDSV RKNLDPFNQH
TDEDLWKALE EVQLKCVVEE LPGKLETVLA ESGSNFSVGQ RQLVCLARAI LRKNRILXID
EATANVDLRT DELIQKTIRD KFRDCTVLTI AHRLNTIIDS DRILVLDSGT IQELDCPFTL
LQNKEGALYK MAQETGHAEA AALLESARQV T
//
