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Database: UniProt
Entry: M3YV80_MUSPF
LinkDB: M3YV80_MUSPF
Original site: M3YV80_MUSPF 
ID   M3YV80_MUSPF            Unreviewed;      1206 AA.
AC   M3YV80;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=ATPase 13A1 {ECO:0000313|Ensembl:ENSMPUP00000015240.1};
GN   Name=ATP13A1 {ECO:0000313|Ensembl:ENSMPUP00000015240.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015240.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000015240.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-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   EMBL; AEYP01051370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004760898.1; XM_004760841.2.
DR   AlphaFoldDB; M3YV80; -.
DR   STRING; 9669.ENSMPUP00000015240; -.
DR   Ensembl; ENSMPUT00000015479.1; ENSMPUP00000015240.1; ENSMPUG00000015350.1.
DR   GeneID; 101676538; -.
DR   KEGG; mpuf:101676538; -.
DR   CTD; 57130; -.
DR   eggNOG; KOG0209; Eukaryota.
DR   GeneTree; ENSGT00550000075064; -.
DR   HOGENOM; CLU_001828_4_1_1; -.
DR   InParanoid; M3YV80; -.
DR   OMA; QKTKYVW; -.
DR   OrthoDB; 6047at2759; -.
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:0140567; F:membrane protein dislocase activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0140569; P:extraction of mislocalized protein from ER membrane; IEA:Ensembl.
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; 2.
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; 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; 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   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        68..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1054..1075
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1105..1123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1135..1153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1173..1193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          891..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1206 AA;  132723 MW;  956D47B61DF2F879 CRC64;
     MAAAAAAAVG NAVPCGARPC GARPGGQPKP GPQPPTLLAA GPALIASGDE LVAAVWPYRR
     PALLRRLTVL PFAGLLYPAW LGAAAAGCWG WGSSWVQIPE AALLVLATIC LAHALTVLSG
     HWSVHAHCAL TCTPEYDPSK ATFVKVVPTP NNGSTELVAL HRDEGEDGQE VLSFEFQKIK
     YSYDALEKKR FLPVAFPVGN AFSYYQSNRG FQEDSEIRAA EKKFGSNKAE MVVPDFSELF
     KERATAPFFV FQVFCVGLWC LDEYWYYSVF TLSMLVAFEA SLVQQQMRNM SEIRKMGNKP
     HLIQVYRSRK WRPIASDEIV PGDIVSIGRS PQENLVPCDV LLLRGRCIVD EAMLTGESVP
     QMKEPIEDLN PDRVLDLQAD SRLHVIFGGT KVVQHIPPQK ATTGLKPVDN GCVAYVLRTG
     FNTSQGKLLR TILFGVKRVT ANNLETFIFI LFLLVFAIAA AAYVWIEGTK DPSRNRYKLF
     LECTLILTSV VPPELPIELS LAVNTSLIAL AKLYMYCTEP FRIPFAGKVE VCCFDKTGTL
     TSDSLVVRGV AGLKDGKEVT PVSNIPVETH RALASCHSLM QLDDGTLVGD PLEKAMLTAV
     DWTLTKDEKV FPRSIKTQGL KIHQRFHFAS ALKRMSVLAS YEKLGSTDLC YIAAVKGAPE
     TLHSMFAQCP PDYHHIHTEI SREGARVLAL GYKELGHLTH QQAREIKREA LECNLKFVGF
     IVVSCPLKAD SKAVIREIQN ASHRVVMITG DNPLTACHVA QELHFIEKAQ TLILQPPTEK
     GRPCEWRSID GSVVLPLAKG SPKALALEHA LCLTGDGLAH LQAEDPQQLL RLIPHVQVFA
     RVAPKQKEFV ITSLKELGYV TLMCGDGTND VGALKHADVG VALLANAPER VVERRRRPRD
     SPVLSSSGGR APSRAAKQRS GLPPPEEQLA SQRDRLSQVL RELEDESTPI VKLGDASIAA
     PFTSKLSSIQ CICHVIKQGR CTLVTTLQMF KILALNALIL AYSQSVLYLE GVKFSDFQAT
     LQGLLLAGCF LFISRSKPLK TLSRERPLPN IFNLYTVLTV VLQFCVHFLS LVYLYSEAQA
     RSPEKQEQFV DLYKEFEPSL VNSTVYIMAM AMQMATFAIN YKGPPFMESL PENRPLVWSL
     AVSLLAIVGL LLGSSPDFNS QFGLVDIPVE FKLVIAQVLL LDFCLALLAD RVLQFFLGTP
     KLKVPS
//
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