ID M4AG25_XIPMA Unreviewed; 1196 AA.
AC M4AG25;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=ATPase 13A1 {ECO:0000313|Ensembl:ENSXMAP00000013419.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000013419.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000013419.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000013419.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR RefSeq; XP_005801557.1; XM_005801500.2.
DR AlphaFoldDB; M4AG25; -.
DR STRING; 8083.ENSXMAP00000013419; -.
DR Ensembl; ENSXMAT00000013435.2; ENSXMAP00000013419.1; ENSXMAG00000013346.2.
DR GeneID; 102234429; -.
DR KEGG; xma:102234429; -.
DR CTD; 57130; -.
DR eggNOG; KOG0209; Eukaryota.
DR GeneTree; ENSGT00550000075064; -.
DR HOGENOM; CLU_001828_4_1_1; -.
DR InParanoid; M4AG25; -.
DR OMA; QKTKYVW; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07543; P-type_ATPase_cation; 1.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-type_ATPase.
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; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
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};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
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}.
FT TRANSMEM 53..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1044..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1125..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 133589 MW; 54C630A2BB7B05CC CRC64;
MNDAKKDESM AADGIRGPGE LQMAPSVNHN HNDSGAGDEL VSSVTLYRRR PRLLHGTVLP
FLGVLYPGWV YVWLGVYGAS EYPEAGLLAL AAIGIAHVLT ALSGYWSVHV HCWLTCSKEP
DPKLATLAKV IPTPNNGSAE LVTLQRDQDE NGEKILSFEF QKIRYIFDYN EKKCFLPVAF
PINHPLGHFQ SWRGYQEETE LKVAEKRYGT NRAEMVVPDF LELFKERATA PFFVFQVFCV
GLWCLDEYWY YSVFTLFMLV AFEASLVQQQ MRNMSEIRRM GNKPYMIQVY RNRKWRPISS
DELVPGDIVS IGRSPQDNLV PCDVLLLRGR CIVDEAMLTG ESVPQMKEPV EDLDPERMLN
LQTDSRLHII SGGTKVVQHT PPLKTSAGLK PVDNGCVAYV LRTGFYTSQG KLLRTILFGV
KRVTANNLET FIFILFLLVF AIAAAAYVWV EGTKDLTRNR YKLFLECTLI LTSVVPPELP
IELSLAVNTS LIALAKLYVF CTEPFRIPFA GKVEICCFDK TGTLTSDSLV VRGVAGLREG
KEVMPVSEIP VETHRVVATC HSLVTLDDGQ LVGDPLEKAM LTAADWTLTK DEKVFPRGIK
TQGLKIHQRF HFASALKRMS VLASYEKLGS TELCYISTVK GAPETLRGMF TACPGNYDEV
HREMSREGAR VLALGYKEIG HLSHQQCREI NRDVLECDLQ FAGFMVVSCP LKNDSKAVIK
EIQEASHHVV MITGDNPLTA CHVARELHFI QKDHTLILQP SLNQGQWHWE SIDGTVTVAL
PPPSVSSFVQ QFDLCVTGEG LARLGCDPHL LHTLLPHIQV FARVSPKQKE FVITSLKGLG
YVTLMCGDGT NDVGALKHAQ IGVALLANAP ERMPEKKKRG RDKESATSDF RPVPPASSSV
KLSSRAARQR AMAQREEQLA AQKEKFSQVL RELEEDQVQV VKLGDASIAA PFTSKLSSIQ
CICHVIKQGR CTLVTTLQMF KILALNALVL AYSQSVLYLE GVKFSDFQAT LQGLLLAGCF
LFISRSKPLK TLSRERPLPN IFNLYTVLTV LLQFAVHFCS LVYLYKEAQT RSPPREEQFV
DLYKEFEPSL INSTVYIMSM AMQMATFAIN YKGHPFMESL SENRPLLWSI VLSGLAIVGL
LTGSSPEFNE QFALVEIPTE FKLIIAQVLL VDFVAALLVD RVLQFFLGKG TLRLPS
//
