ID A0A2K5L9B8_CERAT Unreviewed; 1545 AA.
AC A0A2K5L9B8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000009541.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000009541.1}
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; 9531.ENSCATP00000009541; -.
DR Ensembl; ENSCATT00000033389.1; ENSCATP00000009541.1; ENSCATG00000028819.1.
DR GeneTree; ENSGT00940000162673; -.
DR OMA; LCKEQEM; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000028819; Expressed in skeletal muscle tissue and 11 other cell types or tissues.
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 GO; GO:0006869; P:lipid transport; IEA:UniProt.
DR CDD; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF270; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 10; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF12698; ABC2_membrane_3; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 773..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 987..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1046..1068
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1074..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1116..1135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 391..626
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1205..1442
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1156..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 176020 MW; 823AE4F9E5B53897 CRC64;
MNKMASASFM KGRTVIGTPD EETMDIVLPK KYREVVGVIF RDTFSYQLKF NWGYRIPPIK
EHTEYTAHCW AMHGEIFCYL AKYWLNGFVA FQAAINAAII EVTTNHSVME ELTSVIGINM
KMLPFISKGE IMNEWFIFTC LVSFSSFIYF ASLNVARERG EFKKLMTVMG LRESAFWLSW
GLTYVCFIFV MSIFMALIIT SIPIIFHTGF MVIFTLFSLY GLSLIALAFL MSVLIRKPML
AGLAGFLFTV FWGCLGFTVL YRQLPLSLGW VLSLLSPFAF IAGMAQITHL DNYLSGVIFP
DPSGDSYIMI ATFFILAFDA LFYLILTLYF ERVLPDKDGH GDSPLFFLKS SFWSKHQNTH
HEIFENEINS EHSSDDSFEP VSPEFHGKEA IRIRNVKKEY NGKTGKVEAL QGIFFDIYEG
QITAILGHDG AGKSTLLNIL SGLSVSTEGS TTIYNTHLSE ITAMEEIRQN IGFCPQFNFQ
FDFLTVRENL RVFAKIKGIQ PKEVEQEVKR IIMELDMQSI QDIIAKKLSG GQKRKLTLGI
AILGDPQVLL LDEPTAGLDP FSRHRVWSLL KEHKVDRVIL FSTQFMDEAD ILADRKVFLS
KGKLKCAGSS LFLKRKWGIG YHLSLHRNEM CDTEKITSLI KQHIPDAKLT TESEEKLVYS
LPLEKTNRFP DLYSDLDKCS DQGIRNYGVS MTTLNEVFLN LEGKSAINEP DFDIGKQKKI
YVTRNTGNES EMEQVLCSLP ETRKAVSSAT LWRRQIYAVA TLRFLKLRRE RRVLLCLSLV
LGVAFIPIIL EKIMYKVFLE THCWEFSPSM YFLSLEQIPK TPLTSLLIIN NTGSNIEDLV
HSLKRQDIVL EIDDFRNRNG SDDPSYNGAI IVSGDQKDYR FSVACNIKKL NCFPVLMGIV
SNALIGIFNF TELIQTESTS FSHDDIVLDL GFIDGSIFLL LITNCISPFI GMSSISDYKK
KVQSQLWISG LWPSAYWCGQ ALVDIPLYFL ILLSIHLIYY FIFLGFQLSW ELVFVLVVCI
IGCAASLIFL TYVLSFIFRK WRKKNGFWPF GFFIILICVS TILVSTQYET PNLILYMIFI
PSFTLLGYIM FLIQFSLMYM RNLDSLDSRI NEVNKTILLT TLIPYLQSLI FLFVIRCLEM
KYGNEIMNKD PVFRISPRSR ETHPNPEEPE EEDEDVQAER VQAANTLTTP NLTEEPVITA
SCLHKEYYDT KKSCFSTRKK KIAIRNVSFC VKKGEVLGLL GHNGAGKSTS IKMITGYTKP
CAGVVVLQDS RTSVRQQHDN SLKFLGYCPQ ENSLWPKLTM KEHLELYAAV KGLGKEDAAL
SISRLVEALK LQEQLKAPVK TLSEGIKRKL CFVLSILGNP SVVLLDEPFT GMDPEGQQQI
WQILQATIKN KERGALLTTH YMSEAEAVCD RVAIMVSGTL RCIGSIQHLK NKFGKDYLLE
IKMKEPTQVE ALHTEILKLF PQAARQERYS SFMAYKLPVE DVHPLSRAFF KLEAVKQAFN
LEEYSLSQAT LEQVFLELCK EQEMGNVDDK IDTTVQWKLL PQEDP
//
