ID A0A3Q2ZVC6_KRYMA Unreviewed; 1505 AA.
AC A0A3Q2ZVC6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000007836.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000007836.1}
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 RefSeq; XP_017279688.1; XM_017424199.1.
DR RefSeq; XP_017279689.1; XM_017424200.1.
DR STRING; 37003.ENSKMAP00000007836; -.
DR Ensembl; ENSKMAT00000007959.1; ENSKMAP00000007836.1; ENSKMAG00000005839.1.
DR GeneID; 108240610; -.
DR KEGG; kmr:108240610; -.
DR CTD; 538; -.
DR GeneTree; ENSGT00940000159568; -.
DR OMA; PNSWISG; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000264800; 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:SF29; COPPER-TRANSPORTING ATPASE 1; 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:UP000264800};
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 662..681
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 712..734
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 755..776
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 782..804
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 947..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 994..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1365..1387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1393..1413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 8..74
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 176..242
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 285..351
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 384..450
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 496..562
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 572..638
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 150..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 162914 MW; D19514F654BDDABE CRC64;
MTHKVNLCSV SLRIEGMTCG SCVQSIEQRI GFLSGVIHIK VSLEQQSATI IYDHSLQSPE
SLVEAIEDMG FDSSMPESST ATPLSTDTHL IPTSSLTPAA QQEALEKLSQ IQGVLDVRES
LPQTGLTVTF IPSLTSVQQL REVVDGATPL EIQTPGSPSQ KGLKLSPSHT GGDRAAILKL
SIEGMTCHSC TTTIEGKIGK LKGIEKIKVI LDSQEATVVY LPYLISVQTI IDQIAVAGFK
ASVRSKPRPL QLSPREIERF VDSQKAAASS SSESSEETEV FIDTVLVMLR VKGMHCRSCV
VNIQDNISKL PAVSSVEVFL EKEKASICYD PLQITVAELQ RAIEALPPGN FKTEPWDSPY
ALSPASAPPA SSAAQLCFTQ PLNSVVHIHI EGMTCNSCVE SIERMISQRK GVMSTRVSLI
DHQGTFEYDP LLTSPEELRE AIEDMGFDAM LPETNSLLPV PELGFSRSPS TAPVQEELDN
DHHSKPPQGQ TGDVPSKCYI QIGGMTCASC VANIERNLKN EHGIYSVLVA LMAGKAEVRY
DPKVTDPLKV AESIKELGFT ASVMENYEGS NGNLELVVRG MTCASCVHKI ESSLVKEKGI
IYASVALATN KAHVKYDSEI IGPRDIIKLI EKLGFEASLV KRDRTGSHLD HSKEIRQWRK
SFLVSLIFCV PVMGMMIYMI IMDHQMSVSH HHNATEEDRN HYHSSMFLET QLLPGLSIMN
LLSFIFCVPV QFIGGRYFYV QAYKALKHKS ANMDVLIVLA TSIAFSYSCV ILLVAMVEKA
KINPITFFDT PPMLFVFISL GRWLEQIAKS KTSEALSKLM SLQATEATVV TLSSDNAILS
EEQVDVDLVQ RGDVVKVVPG GKFPVDGRVI EGHSMADESL ITGEAMPVTK KPGSSVIAGS
INQNGSLLVS ATHVGQDTTL SQIVKLVEEA QTSKAPIQQY ADKISGYFVP FIVGISLLTL
VAWVVIGFLD FSLVESIFPG YDKSISRAEV VLRFAFQASI TVLCIACPCS LGLATPTAVM
VGTGVGAQNG ILIKGGEPLE MAHKVQSVVF DKTGTITYGA PKVVQVKIVV EGNKMPRSRL
LAIVGTAENN SEHPLGAAIT RYCKQELSTE SLGTCTDFQA VPGCGIRCQV SNTETLLKQL
DSDGEDNVQR NSVLVQISDT LTATSSHPLI MDPQPLSLVQ TATFVVLIGN REWMRRNCLN
VSPEVNEAMV EHERRGRTAV LVAVDNELCA MIAIADTVKP EAKLAVDTLT SMGLEVVLMT
GDNSKTARAI AAQVGIRKVF AEVLPSHKVA KVEQLQQTGM RVAMVGDGVN DSPALAMADI
GIAIGTGTDV AIEAADVVLI RNDLLDVVGS IDLSKKTVKR IRINFIFALI YNLVGIPIAA
GVFLPIGLVL QPWMGSAAMA MSSVSVVVSS LLLKCYTKPT AEKLEAKFGS GTRQGSLSDV
SVHIGMGDVR RPSPKLSLLD RFVNYSRASI NSLRSDKHSL NSLALNEPDK HSLLVEETLC
EEEFC
//
