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Database: UniProt
Entry: A0A2K6SDA9_SAIBB
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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}.
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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
//
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