ID A0A452HUI6_9SAUR Unreviewed; 1439 AA.
AC A0A452HUI6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000018727.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000018727.1}
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|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; 38772.ENSGAGP00000018727; -.
DR Ensembl; ENSGAGT00000021348.1; ENSGAGP00000018727.1; ENSGAGG00000013855.1.
DR Proteomes; UP000291020; 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:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR CDD; cd00371; HMA; 5.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 5.
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; 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; 5.
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; 5.
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; 5.
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:UP000291020};
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 594..613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 651..672
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 684..708
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 720..737
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 880..904
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 924..947
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1298..1323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1329..1349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 103..169
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 210..276
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 313..379
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 429..495
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 504..570
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1439 AA; 156597 MW; EB2C414018A535C1 CRC64;
MGFDATLADS DPQPVLLDTT FLTIPTQSHV TCEQICNALL KNKGILDVKI SSDQKTAVVS
FISSIINGNQ IIQMVPGIDL NTAAPEKTSG TEEDSSWSQA CDVVLRMKVE GMTCHSCTST
IEGKIGKLQG VQRIKVSLDN QEAVIVYQPH LITAEEIKNQ IEAAGFTAII KKQPKPIKLG
VIDVARLKNT QTKSSEGTLQ RSPKHINDLK AIVFRIEGMH CNSCVLNIQS SISALPSVAS
IVVSLEKKTA TVKYNPDFIS IDALRRAIEA VSPGTFKVSL PDEYENVELF SAQISPMKPS
QTALNSTNQS VTQVTVVNIE GMTCNSCVQS IEEVISRKPG VKSICVSLVN HNGTIKYDPL
LTCPEDLKSA IEDMGFDASL SAKTEPLVLI TQPSLEVSLD SQDNMVYITA PHSKVSPVHD
DKQEAKTPSK CYIQVTGMTC ASCVANIERN LRREDGICSV LVALMAGKAE VRYDPAIIQP
SVIAGLIREL GFGATVMENY DGDGILELVV RGMTCASCVH KIESTLMKTK GVLYSSVALA
TNKAHIKYDP EIVGPRDIIQ TVEDLGFETS LVKKDRSAGH LDHKQEIRQW KRSFLVSLFF
CIPVMALMIY MMVMDSHLAD VHQHRNMSKE EMEAYHSSMS LEHQVLPGLS VMNLLSFLLC
VPVQLFGGWY FYIQAYKALK HKTANMDVLI VLATTIAFVY SFVVLLVAMV EKAKVNPVTF
FDTPPMLFVF IALGRWLEHM AKGKTSEALS RLISLQATEA TLVNLGPDNI LLSEDQVDVE
LVQRGDIVKV VPGGKFPVDG CVIEGQSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL
LISATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVAVSV LTLFAWIVIG
FVNFEIVETY FHGYNKSISK TEVVIRFAFQ AAITVLCIAC PCSLGLATPT AVMVGTGVGA
QNGILIKGGE PLEMAHKVKV VVFDKTGTIT HGTPVVMQVK ILVEDNQMPR NKILAIVGTA
ESNSEHPLGT AITKYCKKEL DSESLGTCTD FQVVAGCGIS CKVTNIEELL YRRNEKVEEN
NIKNITFIKV DENFEDPMQP ALIIDAQLPT TLNHQKYSVL IGNREWMNRN GLLLKSNIDN
AMIEHERRGC TAVLVAVDGV LCGLIAIADT VKPEAELAVH ILKTMGLEVV LMTGDNSKTA
RYIASEVGIT KVFAEVLPSH KVAKVKQLQE EGKRVAMVGD GINDSPALAM ANVGIAIGTG
TDVAIEAADV VLIRNDLLDV VASIDLSRKT VRTIRFNFVF ALIYNLVGIP VAAGVFLPVG
IILQPWMGSA AMAASSVSVV CSSLLLKFYK KPNYEKYELR ACGYMRRKSC SEICVHVGID
DTGTASPKLS LMDQIISYSR ASLNSLFSDK RSLNSLVLSE PDKRSLLVGD FREEEDTAL
//
