ID F7GGW1_CALJA Unreviewed; 1529 AA.
AC F7GGW1; U3BUE1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 24-JAN-2024, entry version 66.
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:ENSCJAP00000015472.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000015472.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000015472.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000015472.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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 Ensembl; ENSCJAT00000016346.5; ENSCJAP00000015472.5; ENSCJAG00000008347.5.
DR GeneTree; ENSGT00940000155749; -.
DR OMA; NSWISGT; -.
DR Proteomes; UP000008225; Chromosome 1.
DR Bgee; ENSCJAG00000008347; Expressed in liver and 6 other cell types or tissues.
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:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 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; IPR008250; ATPase_P-typ_transduc_dom_A_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; 6.
DR PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR46594:SF4; P-TYPE CATION-TRANSPORTING ATPASE; 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; SSF81653; Calcium ATPase, transduction domain A; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 6.
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:UP000008225};
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 669..688
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 708..730
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 742..768
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 774..795
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 938..962
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 982..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1389..1411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 73..139
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 158..224
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 272..338
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 374..440
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 503..569
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 579..645
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1496..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1529 AA; 164326 MW; 009DFF9D1F87EFF2 CRC64;
MTPSHGQNYE VPLKVNFLLF QPFPSRPSAQ PQMLSKLSLP TRAWEPAMKK SFAFDNVGYE
GGLDGLGPSS QVTTSTIRIL GMTCQSCVKS IEDRISSLKG IVSVKVSVEQ GSATVNYVPS
VLSPQQVCHQ IGDMGFEASI AEGKAASWPS RSLPAQEAVV KLRVEGMTCQ SCVSSIEGKV
RKLQGVVRVK VSLSNQEAVI TYQPYLIQPE DLRDHVNDMG FEAAIKNKVA PLSLGPIDIE
RLQSTYPKRL FTSANQNINN SETLGNQGNH VVTLQLRIDG MHCTSCILSI EENIGQLPGI
QSIQVSLENK TAQVQYDPSC TSPVSLQRAI EALPPGNFKV SLPDGAEGCG TDHGPFSCHS
PGFSQRNQVQ GTCSTTVIAI AGMTCASCVH SIEGMISQRE GVQQISVSLA EGTGTVLYNP
SVISPEELSS AIEDMGFEAS VISENCSTNS LGNHSAGNSM VQTIGGVPVS VQEVAPHAGG
LPTIHTPDIL AKSPQSTRAV APQKCFLQIK GMTCASCIST IERNLQNKAG ILSVLVALMA
GKAEIKYDPE VVQPLEIAQL IQDLGFEAAV MEDYTGSDGS IELIITGMTC ASCVHNIESK
LMRTNGITYA SVALATSKAL VKFDPEIIGP RDIIKIIEEI GFHASLAQRN PNAHHLDHKM
EIKQWKKSFL CSLVFGIPVM ALMIYMLIPS SEPHESMVLD HNIIPGLSIL NLIFFILCTF
VQLLGGWYFY VQAYKSLRHR SANMDVLIVL ATSIAYVYSL VILVVAVAEK AERSPVTFFD
TPPMLFVFIA LGRWLEHLAK SKTSEALAKL MSLQAVEATV VTLGEDNLII REEQVPMELV
QRGDIVKVVP GGKFPVDGKV LEGNTMADES LITGEAMPVT KKPGSTVIAG SINAHGAVLI
KATHVGNDTT LAQIVKLVEE AQMSKAPIQQ LADRFSGYFV PFIIIMSTLT LVVWIVIGFI
DFDVVQKYFP NPNKHISQTE VIIRFAFQTS ITVLCIACPC SLGLATPTAV MVGTGVAAQN
GILIKGGKPL EMAHKIKTVM FDKTGTITHG VPRVMRVLLL GDMATLPLRK VLAVVGTAEA
SSEHPLGVAV TKYCKELPEE AFTVSSGKPL RRHLCSRWRQ GLQSALATVP GYHKGMSVSL
AFAQHHQELG TETLGYCTDF QAVPGCGIGC KVSNVEGILA HGGHPPSASH LNEAGSLSEG
KDAAPQTFSV LIGNREWLRR NGLTISNDVS DAMTDHEMKG QTAILVAIDG VLCGMIAIAD
AVKQEAALAV HTLQSMGVDV VLITGDNRKT ARAIATQVGI NKVFAEVLPS HKVAKVQELQ
NKGKKVAMVG DGVNDSPALA QADMGVAIGT GTDVAIEAAD VVLIRNDLLD VVASIHLSKR
TVRRIRINLV LALIYNLVGI PIAAGVFMPI GIVLQPWMGS AAMAASSVSV VLSSLQLKCY
KKPELERYEA QVHGRIKPLT ASQVSVHIGM DDRRRDSPRA TPWDQVSYVS QVSLSSLTSD
KPSRHSATVD DGGDKWSLLL NDRDEEQYI
//