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Entry: A0A6G1B9Y4_CROCR
LinkDB: A0A6G1B9Y4_CROCR
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ID   A0A6G1B9Y4_CROCR        Unreviewed;       904 AA.
AC   A0A6G1B9Y4;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE            EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE   Flags: Fragment;
GN   Name=Atp2c2 {ECO:0000313|EMBL:KAF0884819.1};
GN   ORFNames=FOF47_R16521 {ECO:0000313|EMBL:KAF0884819.1};
OS   Crocuta crocuta (Spotted hyena).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Hyaenidae; Crocuta.
OX   NCBI_TaxID=9678 {ECO:0000313|EMBL:KAF0884819.1, ECO:0000313|Proteomes:UP000475037};
RN   [1] {ECO:0000313|EMBL:KAF0884819.1, ECO:0000313|Proteomes:UP000475037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KB4526 {ECO:0000313|EMBL:KAF0884819.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAF0884819.1};
RA   Yang C., Li F.;
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00024147};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC         Evidence={ECO:0000256|ARBA:ARBA00024147};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
CC         Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024272};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC         Evidence={ECO:0000256|ARBA:ARBA00024272};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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:KAF0884819.1}.
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DR   EMBL; VOAJ01001468; KAF0884819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6G1B9Y4; -.
DR   Proteomes; UP000475037; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006413; P-type_ATPase_IIA_PMR1.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF23; CALCIUM-TRANSPORTING ATPASE TYPE 2C MEMBER 2; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Calcium {ECO:0000256|ARBA:ARBA00022568};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000475037};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT   TRANSMEM        253..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        763..783
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        795..813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        833..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        862..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..98
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KAF0884819.1"
FT   NON_TER         904
FT                   /evidence="ECO:0000313|EMBL:KAF0884819.1"
SQ   SEQUENCE   904 AA;  97819 MW;  8EE3BD5E50A8132A CRC64;
     QIDGHCELKA IEREKAVVAL SPKEASKCHR EDLAKAFYVD LQKGLSEFSV SQRRLVHGWN
     EFVTDSAEPV WKKYLDQFKN PLTVLLLVSA LVSVLTKEYE DAVSIAAAVL IVVTVAFIQE
     YRSEKSLEEL TKLVPPECNC IREGKLQHLL ARDLVPGDVV SLSTGDRIPA DIRLTEVRTS
     LCVEGGARGT LPLSKLLPLT LRSASWVGTR VSGLGRLLSG SSRCPLLQRN GVLAICYPSP
     HTSFQRLTPK PGAHGRALFV SFPGLIMFTG WLQGKQLLSM FTIGVSLAVA AIPEGLPIVV
     TVTLVLGVLR MAKKRVIVKK LPIVETLGCC NVICSDKTGT LTANEMTVTQ LVTSDGLHAE
     VSGVGYNGKG AVCLLPSKEV IKEFNNVSVG KLVEAGCAAN NAVIRKNAVI GQPTEGALLA
     LAMKMDLGDI KDSYVRKKEI PFSSEQKWMA VKCSPKNEDQ EDIYFMKGAF EEVINYCTTY
     NHGGISLPLT PQQRAFCQQE EKKMGSLGLR VLALASGPEL GRLTFLGLVG IIDPPRAGVK
     EAMQVLCQSG VSVKMITGDA VETASAIGRS IGLCNGTLKA MSGEEVDSME PKELADHVGK
     VSVFFRTSPK HKLKIIKALQ ESGAIVAMTG DGVNDAVALK SADIGIAMGQ AGTDVSKEAA
     AMILVDDDFS AIMNAVEEGK GIFHNIKNFV RFQLSTSISA LSLITLSTVC KLPSPLNAMQ
     ILWINIIMDG PPAQSSLGVE PVDDDALRQP PRNIKDTILS RALVLKTLLS AAVIISGTLF
     IFWKEIPADK ASTPRTTTMT FTCFVFFDLF NALTCRSQTK LIFEIGFLRN PMFLYSVLGS
     LLGQLAVIYI PPLQKVFQTE NLGALDLLLL TVLASSVFVF SELLKLCEKF CSRAGNAQTR
     REDV
//
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