ID A0A4D9EBF6_9SAUR Unreviewed; 1541 AA.
AC A0A4D9EBF6;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=DR999_PMT09585 {ECO:0000313|EMBL:TFK07537.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK07537.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK07537.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK07537.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK07537.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK07537.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK07537.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK07537.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TFK07537.1}.
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 EMBL; QXTE01000082; TFK07537.1; -; Genomic_DNA.
DR STRING; 55544.A0A4D9EBF6; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 4.
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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
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:ARBA00022796};
KW Kinase {ECO:0000313|EMBL:TFK07537.1};
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:UP000297703};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:TFK07537.1};
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:ARBA00022796}.
FT TRANSMEM 722..741
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 761..783
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 795..821
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 827..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 991..1015
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1035..1058
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1404..1426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 124..190
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 209..275
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 320..386
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 423..489
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 556..622
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 632..698
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1541 AA; 165907 MW; 78FE40209904DF52 CRC64;
MKRESDSDLK RDQSTLATLN NKNVTLVTFH KRQSSNAVPA LLIVSEPSKS GSPGKAGDCS
QKEEKVSQSY SVGASEVNSM HALSKSSSPA SCVREPIMKQ NFAFDNIGYE GSAENMPSLL
PQTSTVTVNI LGMTCQSCVQ SIEGRISKVK GIVSIKISLE QSNAVIKYIQ SEIGPQEICQ
EIGEMGFDAS IAEGRTTASP VRSTSLGEAL MKLRVEGMTC QSCVNTIEGK IGKLHGVLRI
KVSLSNQEAV IAYQPYIIHP EDIKNHIDNM GYESTIKSKL APLKLGMIDL ERLQTTSTKK
TPASLNNSNV EPVVGKMNST TMTLGVEGMH CKSCVKNIEG NISGLPGIHS IKVSLEHKNA
VVQFNPNVIT PVSLQQAIEA LPPGNFKVSL PNGVEANNGE LLSKAAFSSP QFRSTSSGDQ
LTSTSVLSID GMTCGSCVQS IEGTMSQRKG VQHISVSLAE RTGTIHYNSA VTNSEELRGA
IEDMGFDASI LTDTTTWKYM DQPLFRDAVI QPNAWESASQ RTENVSESSH QGYYSDVQPK
NSYLGSPKPP SLATTEKCFM QITGMTCASC VSNIERNLQK EDGIVSVLVA LMAGKAEIKY
KPESIQPLEI VQLIQNLGFN ATVIEDHTAT DGNVELIITG MTCASCVHNI ESKLTRTNGI
FYASVALATS KAHIQFDPEI IGPRDIIQII EGIGFHASLA KRDPNAHNLD HKKEIKQWRK
SFLCSLVFGI PVLILMIYML IPDGQQHSTM VLEQNLIPGL SILNLLFFVL CTLVQFLGGW
YFYVQAYKSL KHKTANMDVL IVLATTIAYI YSCVILVVAI AEKAEESPVT FFDTPPMLFV
FISLGRWLEH IAKSKTSEAL AKLMSLQATE ATIVTLGPDH SVIREVQLAV ELVQRGDIVK
VVPGGKFPVD GKVIEGSSMA DESLITGEAM PVTKKPGSTV IAGSINAHGS VLVNATHVGS
DTTLAQIVKL VEEAQMSKAP IQQLADKFSG YFVPFIIIIS TVTLLVWITI GFINFDVVQK
YFPHQNKHLS KAEVILRFAF QTSITVLCIA CPCSLGLATP TAVMVGTGVA AQNGILIKGG
KPLEMAHKIK TVMFDKTGTI TCGVPKVIRM LLLGDMAKLS LKKVLAIVGT AEASSEHPLG
MAVTKYCKEE LGTESLGYCT DFQAVPGCGI SCKVRSVEAV LGQSEQSVNE QNAYLSSVSM
ISLGHSSSIM VSESDGAAAP LTYSVLIGNR EWMRRNGLLI SSDVNDAMTG HEMKGQTAIL
VAIDGALCGM IAIADTVKQE AALAVHTLQN MGIDVVLITG DNRKTAKAIA TQVGIKKVFA
EVLPSHKVAK VQELQNEGKK VAMVGDGVND SPALAGADIG IAIGTGTDVA IEAADVVLIR
NDLLDVVASI HLSKRTVRRI RINLVLALIY NLLGIPIAAG VFMPIGIVLQ PWMGSAAMAA
SSVSVVLSSL QLKCYKKPGT ERYEAKAQGH MKPLTPSQIS VHIGMDDRRR DSPRPTAWDQ
ISQVSLSSLT SNKLPGHGGF REEEGGKWSL LTNNRDEEQY I
//