UniProt: A0A1L8GAB2

Database: UniProt
Entry: A0A1L8GAB2_XENLA

LinkDB:  A0A1L8GAB2_XENLA 
Original site:  A0A1L8GAB2_XENLA

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Ontology (6)   
   GO (6)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (26)   

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ID   A0A1L8GAB2_XENLA        Unreviewed;      1202 AA.
AC   A0A1L8GAB2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE            EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN   Name=atp13a5l.2.L {ECO:0000313|RefSeq:XP_018119094.1,
GN   ECO:0000313|Xenbase:XB-GENE-22167923};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018119094.1};
RN   [1] {ECO:0000313|RefSeq:XP_018119094.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018119094.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018119094.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|RuleBase:RU362082};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362082}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362082}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC       ECO:0000256|RuleBase:RU362082}.
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DR   RefSeq; XP_018119094.1; XM_018263605.2.
DR   AlphaFoldDB; A0A1L8GAB2; -.
DR   STRING; 8355.A0A1L8GAB2; -.
DR   PaxDb; 8355-A0A1L8GAB2; -.
DR   GeneID; 108716978; -.
DR   KEGG; xla:108716978; -.
DR   AGR; Xenbase:XB-GENE-22167923; -.
DR   CTD; 108716978; -.
DR   Xenbase; XB-GENE-22167923; atp13a5l.2.L.
DR   OrthoDB; 6047at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 108716978; Expressed in camera-type eye and 7 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
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; 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; IPR006544; P-type_TPase_V.
DR   InterPro; IPR047819; P5A-ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   NCBIfam; TIGR01657; P-ATPase-V; 1.
DR   PANTHER; PTHR45630:SF1; CATION-TRANSPORTING ATPASE 13A4-RELATED; 1.
DR   PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF12409; P5-ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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; 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, ECO:0000256|RuleBase:RU362082};
KW   Magnesium {ECO:0000256|RuleBase:RU362082};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW   Metal-binding {ECO:0000256|RuleBase:RU362082};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362082};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362082}.
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        194..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        217..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        424..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        897..921
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        933..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        971..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1029..1050
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1062..1084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1096..1118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   DOMAIN          12..133
FT                   /note="P5B-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12409"
FT   DOMAIN          152..201
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
SQ   SEQUENCE   1202 AA;  135405 MW;  7A5EA95AFAFF6D30 CRC64;
     MTAKYALLNQ GEDNEMEVFG YKTVRWQQVL CIIGYIFSLG FLRVLFYWKP QLDVWCQCIP
     CSFSQADVIL LRTTDDHREF SKKKVIEISP RTQGSKSDHQ TITKKNSIID KSLMKPMGKI
     RYIEAQKIRY VWNTVEGKFQ KIGILEEDLS CSDIHSKFGS GLTAEEQEIR QQVCGLNSIE
     VEIKPIWIIL IKEIFNPFYV FQVYSLSIWM WCAYVEYSCV ILAMSILSII ATVYNLRVQS
     VKLHKMSISY NSIMVTVLRK NGELKEVESQ TLVPGDVIIL YISENKHFLP CDAILINGAC
     TVNEGMLTGE STPVSKVPLP RIESSMPWKM QCGEDYKRHV LFCGTEVIQI KAYGQDLVKA
     VVIQTGFNTT KGDLVRAILY NKPMNVKLHR EAMRFLLVLV FISLLGVAYS AAVFKKNGAS
     VHEIVMMSLL ILTLAVNATL PASLTLGLLY GQTRLKKLGI FCISPQRIIL AGQLNLVCFD
     KTGTLTEDSL DLHGVLPSNG TSFQDIHLFS SAKTMPWSPL LGAMASCHSL IMEDGKMQGD
     PLDLKMFEGT GWEFESHAAQ GTKDGESNSY TMVKPGPSAG EVPVEGIAVL HQLPFSSSLQ
     RMSVITQILG ERDFTVFMKG APEMVIRFCK PETVPHNISK KLDYYTTQGF RVIGLAYRLL
     QKEGIPAIED LKWDIIETDL IFLGLLILEN RLKPETITVL QELSTAKIRN VMVTGDNLQT
     ALNIGKHCGM IPKSSKIIII EASEPQNDVP ASITWKTITE NQENEHKETF QSFHTVINAG
     WKPNTSQPEE FHFAIDGKSF QILRQHFYNI VPKVLLNGTI FARMTPKLKS SLVEEFRKLE
     YHVGMCGDGA NDCGALKMAN VGVSLSELEA SVASPFTSKI PNIQCVPMLI KEGRNTLVSS
     FSMFKFLSVL TTVGLLSMVF LFWKQTFLSN AQYLMQDCAI VIPVCLTASL NGPAPKLAPH
     RPPGQLLSPS LLLSVFLHFL LSLGLQTTAY VLLQAQPWYN ESDVFSACLP LNHSTENITA
     RVPTITETYL ATTTWIVTGM NIITIEFVFA KGSPFRQRLH TNYLFIIIII LQVAIFLFFL
     FAGFEQIYTT FEVVCIPFYW RVYILVMVLV HFVLSYAIEE GILENRKLWL LIKKLCNYQS
     KSQYRKLQRG LKMDTEWPPQ NRTDYAIKSA SVVDSKILVF KNASYQPPTE NSGEFLGPQK
     IM
//

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