AT8B3_MOUSE
ID AT8B3_MOUSE Reviewed; 1335 AA.
AC Q6UQ17;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phospholipid-transporting ATPase IK {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000269|PubMed:14975727};
DE AltName: Full=ATPase, class I, type 8B, member 3;
DE AltName: Full=Sperm aminophospholipid transporter;
DE Short=SAPLT;
GN Name=Atp8b3 {ECO:0000312|MGI:MGI:1914581};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=ICR; TISSUE=Testis;
RX PubMed=14975727; DOI=10.1016/j.ydbio.2003.11.004;
RA Wang L., Beserra C., Garbers D.L.;
RT "A novel aminophospholipid transporter exclusively expressed in spermatozoa
RT is required for membrane lipid asymmetry and normal fertilization.";
RL Dev. Biol. 267:203-215(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP FUNCTION.
RX PubMed=19017724; DOI=10.1530/rep-08-0048;
RA Gong E.Y., Park E., Lee H.J., Lee K.;
RT "Expression of Atp8b3 in murine testis and its characterization as a testis
RT specific P-type ATPase.";
RL Reproduction 137:345-351(2009).
CC -!- FUNCTION: P4-ATPase flippase which catalyzes the hydrolysis of ATP
CC coupled to the transport of aminophospholipids from the outer to the
CC inner leaflet of various membranes and ensures the maintenance of
CC asymmetric distribution of phospholipids (PubMed:14975727,
CC PubMed:19017724). Phospholipid translocation seems also to be
CC implicated in vesicle formation and in uptake of lipid signaling
CC molecules (PubMed:14975727). May be responsible for the maintenance of
CC asymmetric distribution of phosphatidylserine (PS) in spermatozoa
CC membranes (PubMed:14975727). Involved in acrosome reactions and binding
CC of spermatozoa to zona pellucida (PubMed:19017724).
CC {ECO:0000269|PubMed:14975727, ECO:0000269|PubMed:19017724}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:14975727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:14975727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000305|PubMed:14975727};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000269|PubMed:14975727, ECO:0000269|PubMed:19017724};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:O60423}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, specifically in spermatids
CC within seminiferous tubules (at protein level).
CC {ECO:0000269|PubMed:14975727, ECO:0000269|PubMed:19017724}.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated in testis. Expression is
CC first detected at 17 days after birth and is later up-regulated up to
CC adulthood amd maintained thereafter. {ECO:0000269|PubMed:19017724}.
CC -!- DISRUPTION PHENOTYPE: Disrupted normal fertilization by sperm;
CC sensitivity to sperm concentration and the time required to fertilize
CC an egg is increased; the number of spermatozoa bound to zona pellucida
CC is decreased. {ECO:0000269|PubMed:14975727}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; AY364445; AAR12913.1; -; mRNA.
DR EMBL; AC152058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118977; AAI18978.1; -; mRNA.
DR CCDS; CCDS24024.1; -.
DR RefSeq; NP_080370.2; NM_026094.3.
DR AlphaFoldDB; Q6UQ17; -.
DR SMR; Q6UQ17; -.
DR STRING; 10090.ENSMUSP00000020383; -.
DR SwissLipids; SLP:000000353; -.
DR iPTMnet; Q6UQ17; -.
DR PhosphoSitePlus; Q6UQ17; -.
DR MaxQB; Q6UQ17; -.
DR PaxDb; Q6UQ17; -.
DR PRIDE; Q6UQ17; -.
DR ProteomicsDB; 277087; -.
DR Antibodypedia; 67630; 55 antibodies from 11 providers.
DR DNASU; 67331; -.
DR Ensembl; ENSMUST00000020383; ENSMUSP00000020383; ENSMUSG00000003341.
DR GeneID; 67331; -.
DR KEGG; mmu:67331; -.
DR UCSC; uc007gdo.1; mouse.
DR CTD; 148229; -.
DR MGI; MGI:1914581; Atp8b3.
DR VEuPathDB; HostDB:ENSMUSG00000003341; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000160463; -.
DR HOGENOM; CLU_000846_3_2_1; -.
DR InParanoid; Q6UQ17; -.
DR OMA; HNELTSH; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q6UQ17; -.
DR TreeFam; TF300654; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 67331; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Atp8b3; mouse.
DR PRO; PR:Q6UQ17; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6UQ17; protein.
DR Bgee; ENSMUSG00000003341; Expressed in spermatid and 20 other tissues.
DR ExpressionAtlas; Q6UQ17; baseline and differential.
DR Genevisible; Q6UQ17; MM.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IMP:MGI.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030349; ATP8B3.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR24092:SF78; PTHR24092:SF78; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasmic vesicle; Endoplasmic reticulum; Lipid transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1335
FT /note="Phospholipid-transporting ATPase IK"
FT /id="PRO_0000429839"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..295
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..917
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 918..938
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 939..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 947..967
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 968..995
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1034..1054
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1055
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1077..1104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1126..1335
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT REGION 1192..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 857
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 861
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1335 AA; 151955 MW; 7674AA921B28EE35 CRC64;
MDGVHLGENL EDKDTEFTWE VKANDRTYHK QFKKKGFLCW RQKKYKSNAI HTAKYNIFSF
LPLNLYEQFH RMSNLYFLFI IILQGIPEIS TLPWFTLFAP LVCLFVIRAT RDLVDDIGRH
RSDKIINNRP CQILRGKSFL WKKWKNLCVG DVVCLSKDSI VPADLLLLAS TEPSSLCYVE
TADIDGETNL KFRQALTVTH HELTSPKKMA SFQGTVTCEE PNSRMHHFVG SLEWNSRKYP
LDIGNLLLRG CKIRNTDTCY GLVIYAGLDT KIMKNCGKIH LKRTKLDLMM NKLVALIFLS
LVIASLLLTV GFTFMVKQFK AKHYYMSPTH GRSDAMESFF IFWGFLILLS VMVPMAMFII
AEFIYLGNSI FINWDLNMYY EPLDMPAKAR STSLNDQLGQ VQYIFSDKTG TLTQNIMTFK
KCCINGCIYD SDDEHGTLRK RNPYAWNPFA DGKLQFYNKE LESLVQGRQD RAVQEFWRLL
AICHTVMVQE KDNQLLYQAA SPDEEALVTA ARNFGYVFLS RTQDTITLVE LGEERVYQVL
AMMDFNSVRK RMSVLVRNPE GSICLYTKGA DTVILERLRS KGVMEATTEE VLAAFAEQTL
RTLCLAYKDV EEDAYKEWEP EHQEAALLLQ NRAQALHQVY NKMEQNLQLL GATAIEDKLQ
DGVPETIKCL KKGNIKIWVL TGDKPETAVN IGFACQLLSE NMIILEDKDI NQVLERYWED
NVHQKAFKMM THHNMALVIN GEFLDQLLLS LRKEPRALVQ NAVVDEVAQE PVVSALDFLQ
KRRISQMWRN AGPSLGTSHS ADSKIRESPE VQRERAFVDL ASKCQAVICC RVTPKQKALV
VALVKKYQQV VTLAIGDGAN DVNMIKTADI GVGLAGQEGM QAVQNSDYVL AQFCYLQRLL
LVHGRWSYMR VCKFLRYFFY KTVASMMAQI WFSLVNGFSA QPLYEGWFLA LFNLLYSTLP
VLYIGLFEQD VTAEKSLKMP ELYMAGQKGE LFNYSIFMQA ITHGTITSMI NFFVTVMVSS
DMSKAGSSHD YQSLGVLVAI SSLLSVTLEV MLVVKYWTLL FVGAVVLSLS SYVLMTSLTQ
SLWMYRISPK TFPFLFADYN VLFEPCSLLL IVLNVALNVL PMLALRTIHR TVLKQRPKGE
EEAPSEEVAV EPAMRHLRRG IPARRSSYAF SHREGYANLI TQGTILRRQT HVDDSDGGTV
CESLNPPEED IPLQNKDSVF NPRKISILAK KRRHFFGKGS QEEVHPNTSS QTMEKQPTIH
RDSETQKLPT TTSATSGKLL PSASEDEAFY SVASQYTLAS QPKHTDVHSS FWKSPLWRDS
ASSSPSQLEV PRKQS
