ID H0Z6L2_TAEGU Unreviewed; 1497 AA.
AC H0Z6L2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN Name=ATP7A {ECO:0000313|Ensembl:ENSTGUP00000006210.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000006210.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000006210.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000006210.2}
RP IDENTIFICATION.
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; 59729.ENSTGUP00000006210; -.
DR Ensembl; ENSTGUT00000006271.2; ENSTGUP00000006210.2; ENSTGUG00000005981.2.
DR GeneTree; ENSGT00940000159568; -.
DR HOGENOM; CLU_001771_0_1_1; -.
DR InParanoid; H0Z6L2; -.
DR OMA; PNSWISG; -.
DR OrthoDB; 5480493at2759; -.
DR TreeFam; TF300460; -.
DR Proteomes; UP000007754; Chromosome 4A.
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:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; 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:0032767; F:copper-dependent protein binding; IEA:Ensembl.
DR GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0060003; P:copper ion export; IEA:Ensembl.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; IEA:Ensembl.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; 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; 2.
DR NCBIfam; TIGR00003; copper ion binding protein; 6.
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; 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:ARBA00022796};
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:UP000007754};
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:ARBA00022796}.
FT TRANSMEM 652..671
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 703..725
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 746..768
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 938..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1356..1378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1384..1404
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 4..70
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 167..233
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 273..339
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 375..441
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 486..552
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 562..628
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1497 AA; 161618 MW; 70714061B37388E2 CRC64;
MEAKSVAIGV EGMTCSSCVQ SIEQHLGKMN GIHNIKVSLE DKNALIIYDS KLQTPATLQE
AICDMGFDAT LADSNPQPVL PDTIFLTLPA QSALTPRQIC ATLLSNKGIL DVKVSSDQRT
AVVTFIPSIT NGRHITQMVP GADLSISVPE VTPGTWEDSS WSQVSSAVLR LKVDGMTCHS
CTSTIEGKLG KLQGVQRIRV SLDNKEAVVV YQPPLITPEE IKQQIEAAGF TAAFKKQPRP
LKLSGIDLER LRNAQPRSSE ASQGENSSGT GTKTVVFRVE GMHCNSCVLN IQSTVSALPA
VSSVVVSLEN KSAAINYNPS LISLEKLRKA VENVSPERFR VSLPEEHESL ALFPTLASPL
KSHPPSKDPS QPLSQVVVIN IEGMTCSSCV QSIEGVLSQK AGVKSVHVSL PNGTGTIEYD
PLQTNPEDLR SSIEDMGFDA SFPAKAELPM AKAQPCPEAQ LDSHKPEQPS KVAPAHLGRQ
ESKTISKCYV QVTGMTCASC VANIERNLRR EDGIHSILVA LMAGKAEVRY NPAVIHPAAI
AELIRELGFG ATVMENCGEG DGILELIVRG MTCASCVHKI ESTLMKTSGV LYCSVALATN
KAHIKYDPEA IGPRDVIQVI KDLGFTTSLV KKDRSASHLD HKQEIRQWKR SFVVSLVFCI
PVMGLMIYMM VMDSQLSHAH AHHNMSSEEM EALHSSMVLE YQLLPGLSVM NFLSFLLCVP
VQVFGGWHFY IQASRALRHN TANMDVLVVL ATSIAFLYSF IILLVAMAER AKVNPVTFFD
TPPMLFVFIS LGRWLEHVAK GKTSEALARL ISLQATEATI VTLGPDNVLL SEEQVDVELV
QRGDIVKVVP GGKFPVDGRV IEGHSMVDES LITGEAMPVT KKPGSTVIAG SINQNGSLLI
SATHVGADTT LSQIVKLVEE AQTSKAPIQQ FADKLSGYFV PFIVAVSVVT LFAWIIIGFV
DFEIVEKYFL GYNKSISAAE VIVRFAFQAS ITVLCIACPC SLGLATPTAV MVGTGVGAQN
GILIKGGEPL EMAHRVKVVV FDKTGTITHG TPEVMQVKFL VEGNLLPRHK MLAIVGTAES
SSEHPLGAAI TKYCKKELNS ETLGTCTDFQ VVPGCGISCK VTNIEALLYR KNRMVEENNV
KNVTLVKIEE NTDELVQPAL IIDTELPTTV TSQKYSVLIG NREWMTRNGL LVRNEVDKAM
MEHERRGRTA VLAAVDGVLC ALIAIADTVK PEAELAVYTL KSMGLEVVLM TGDNSKTARS
IASQVGITKV FAEVLPSHKV AKVKQLQDEG KRVAMVGDGI NDSPALAMAN VGIAIGTGTD
VAIEAADVVL IRDDLMDVVA SIDLSRKTVK RIRINFVFAL IYNLIGVPIA AGVFLPIGLV
LQPWMGSAAM AASSVSVVLS SLLLKMYQKP SSEKLEFRAR GQLRHKSPSE ISVRVGIDES
GAGSPKLSLM DRIITYSRAS INSLFSDKRS VNSIVLTEPD KHSLLVGDFG EDDDTAL
//
