ID A0A2K6SDA9_SAIBB Unreviewed; 1387 AA.
AC A0A2K6SDA9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSSBOP00000005372.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000005372.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000005372.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSSBOT00000022006.1; ENSSBOP00000005372.1; ENSSBOG00000019143.1.
DR GeneTree; ENSGT00940000155749; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:UniProt.
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:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; 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; 2.
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; 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 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:UP000233220};
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 654..673
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 688..706
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 845..869
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 889..912
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1247..1269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 58..124
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 143..209
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 257..323
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 359..425
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 488..554
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 564..630
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 326..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 148398 MW; 30050DCC04FEEAAF CRC64;
MPEQERHITA REGASRKILS KLSLPTRAWE PAMKKSFAFD NVGYEGGLDD LGPSSQVTTS
TISILGMTCQ SCVKSIEDRI STLKGIVSVK VSLEQGSATV NYVPSVLSPQ QVCHQIGDMG
FEASIAEGKA ASWPSRSLPA QEAVVKLRVE GMTCQSCVSS IEGKVRKLQG VVRVKVSLSN
QEAVITYQPY LIQPKDLRDH VNDMGFEAAI KNKVAPLSLG PIDIERLQST YPKRPFTSAN
QNFNNSETLG HQGNHVVTLQ LRIDGMHCTS CILNIEENIG QLPGIQSIQV SLENKTAQVQ
YDPSCTSPVS LQRAIEALPP GNFKVSLPDG AEGYGTDHRP SSSHSPGFSQ RNQVQGTCST
AVIAIAGMTC ASCVHSIEGM ISQREGVQQI SVSLAEGTGT VLYNPSVISP EDLSAAIEDM
GFEASVISEN CSTNSLGNHS AGNSMVQITG GVPASVQEVA PHAGGLPTNH TPDILAKSPQ
SARAAAPQKC FLQIKGMTCA SCVSTIERNL QNKAGILSVL VALMAGKAEI KYDPEVVQPL
EIAQLIQDLG FEAAVMEDYA GSDGSIELII TGMTCASCVH NIESKLTRTN GITHASVALA
TSKALVKFDP EIIGPRDIIK IFEEIGFHAS LAQRNPNARH LDHKMEIKQW KKSFLCSLVF
GIPVMALMIY MLIPSNEPHE SMVLDHNIIP GLSILNLIFF ILCTFVQSKT SEALAKLMSL
QAAEATVVTL GEDNLIIREE QVPMELVQRG DIVKVVPGGK FPVDGKVLEG NTMADESLIT
GEAMPVTKKP GSTVIAGSIN AHGTVLIKAT HVGNDTTLAQ IVKLVEEAQM SKAPIQQLAD
RFSGYFVPFI IIMSTLTLVV WIVIGFIDFD VVQKYFPNPN KHISKTEVII RFAFQTSITV
LCIACPCSLG LATPTAVMVG TGVAAQNGIL IKGGKPLEMA HKIKTVMFDK TGTITHGVPR
VMRVLLLGDV ATLPLRKVLA VVGTAEASSE HPLGMAVTKY CKEELGTETL GYCTDFQAVP
GCGIGCKVSN VEGILAHSGC PLSTPASHLN EAGSIPKEKD AAPQTFSVLI GNREWLRRNG
LTISSDVSDA MTDHEMKGQT AILVAIDGVL CGMIAIADAV KQEAALAVRT LQSMGVDVVL
ITGDNRKTAR AIATQVGISK VFAEVLPSHK VAKVQELQNK GKKVAMVGDG VNDSPALAQA
DMGVAIGTGT DVAIEAADVV LIRNDLLDVV ASIHLSKRTV RRIRINLVLA LIYNLVGIPI
AAGVFMPIGI VLQPWMGSAA MAASSVSVVL SSLQLKCYKK PDLERYEAQV HGRMKPLTAS
QVSVHIGMDD RRRDSPRTTP WDQVSYVSQV SLSSLTSDKP SRHSAAVDDG GDKWSLLLND
RDEEQYI
//