ID G3T9F9_LOXAF Unreviewed; 1465 AA.
AC G3T9F9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN Name=ATP7B {ECO:0000313|Ensembl:ENSLAFP00000010415.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000010415.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000010415.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010415.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000010415.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010415.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004166}. Membrane
CC {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR STRING; 9785.ENSLAFP00000010415; -.
DR Ensembl; ENSLAFT00000012463.4; ENSLAFP00000010415.4; ENSLAFG00000012459.4.
DR eggNOG; KOG0207; Eukaryota.
DR GeneTree; ENSGT00940000155749; -.
DR HOGENOM; CLU_001771_0_1_1; -.
DR InParanoid; G3T9F9; -.
DR OMA; MVCPRIH; -.
DR TreeFam; TF300460; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032588; C:trans-Golgi network membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IEA:Ensembl.
DR GO; GO:0015677; P:copper ion import; IEA:Ensembl.
DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR GO; GO:0051208; P:sequestering of calcium ion; IEA:Ensembl.
DR CDD; cd00371; HMA; 6.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 6.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 5.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 6.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 6.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 5.
DR PROSITE; PS50846; HMA_2; 6.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 659..678
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 698..720
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 732..758
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 876..896
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 928..950
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 971..994
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1325..1347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 57..123
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 142..208
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 256..322
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 362..428
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 491..557
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 567..633
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 224..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1465 AA; 157474 MW; 343E34A27038F52B CRC64;
NPAKRVRQTT LERDAEILSR LSLHARAGEP AMKQNFAFDN VGYEGSLDSA SPPSQMATGT
VSILGMTGQS CVKSIEGRIS SLNGIMSIKV SLEQGSATVT HVPSVMSLQQ VCRHIADMGF
EASIAEGKAA SWPCRSSPSG EAVVKLRVEG MTCQSCVSSI EGKIGKLQGV LRVRVSLGNQ
EAVITYQPYL IQPEDLRDHV NDMGFEAAVK NKVAPLSLGP IDIGRLQSTN PKRPSTPAHQ
SLNNSEALGD QESREVTLQL RVDGMRCKSC VLSIEENIGQ LPGVRSIQVS LENRTAQVQF
EPSRISPVSL QKAIEALPPG NFKVQLPDGS EASGTECLPD VRPSELRSCD SSQRNHKHGV
HSSVVLTIAG MTCASCVQSI EGVISQREGV QQISVSLTEG TGTILFNSAL INPEELRAAV
EDMGFEACII SENSSSSHVG SHGSANSRVQ TTGGISLSVQ EAALHARGLP PSHNPGHSSV
SQQSSGTVVP QKCFLQISGM TCASCVSNIE RNLQKEAGVL SVLVALMAGK AEVKYNPEII
QPFEIAQLIE NLGFQAAVME DYTGSDGNIE LSIRGMTCAS CVHNIESKLT KTNGITYASV
ALATSKAHIK FDPEIIGPRD IIKIIENKEI GFHASLAQRD PNAHHLDHKL EIKQWRKSFL
CSLVFGIPVM GLMIYMLIPV HEPHASMALD YNIIPGLSIL NLVFFILCTF VQFLGGWYFY
VQAYKSLKHR AANMDVLIVL ATSIAYVYSL VILVVAIAEK AERSPVTFFD TPPMLFVFIA
LGRWLEHVAK SKTSEALAKL MSLQATEATV VTLGEDNIII SREGHAPRTA EVGLSSPVVP
PEQGPNIEDK NKNGRTSGAA SNVESESMNS AQKPSLLIIC TTVGLHSLAS FIYSNILNEH
MCLKISKTSR EGMHKAPIQQ LADRFSGYFV PFIIIISTLT LVVWIIIGFI DFGVVQKYFP
IPSKHISRAE VILRFAFQTS ITVLCIACPC SLGLATPTAV MVGTGVAAQN GILIKGGKPL
EMAHKIKTVM FDKTGTITHG VPKVMRVLLL VDMAALPLRK VLAVVGTAEA SSEHPLGVAV
TKYCKEELGT ETLGYCTDFQ AVPGCGIGCK VSSVDSILSP STQAHHLNGV GSTPAEKDTA
PETFSVLIGN REWMRRNGLT ISSDISDMMT DHEMKGQTAV LVAIDGVLCG MITIADAVKQ
EAALAVHTLK SMGVDVVLIT GDNRKTARAI ATQVGINKVF AEVLPSHKVA KVQELQNQGK
KVAMVGDGVN DSPALAQADV GIAIGTGTDV AIEAADVVLI RNDLLDVVAS IHLSKRTVWR
IRINLVLALI YNLVGIPIAA GVFMPIGIVL QPWMGSAAMA ASSVSVVLSS LQLKCYRKPD
LEQYEAQAQG RMKPLTPSQV SVHIGMDDRR RDSPWATPWD QVSYVSQVSL SSLTSDRLSR
HSAGADDAGD KWSLLLSDRD EEQYI
//
