AT8B5_MOUSE
ID AT8B5_MOUSE Reviewed; 1183 AA.
AC A3FIN4; A2AIL8; Q8BVE9; Q8BVS7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phospholipid-transporting ATPase FetA;
DE EC=7.6.2.1;
DE AltName: Full=ATPase class I type 8B member 2-like protein;
DE AltName: Full=ATPase class I type 8B member 5;
DE AltName: Full=Flippase expressed in testis A;
GN Name=Atp8b5; Synonyms=Feta;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=19657017; DOI=10.1242/jcs.047423;
RA Xu P., Okkeri J., Hanisch S., Hu R.Y., Xu Q., Pomorski T.G., Ding X.Y.;
RT "Identification of a novel mouse P4-ATPase family member highly expressed
RT during spermatogenesis.";
RL J. Cell Sci. 122:2866-2876(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Gonad, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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).
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. Phospholipid translocation
CC seems also to be implicated in vesicle formation and in uptake of lipid
CC signaling molecules. May play a role in phospholid transport across
CC membranes and in acrosome formation. {ECO:0000269|PubMed:19657017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000269|PubMed:19657017}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19657017}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A3FIN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3FIN4-2; Sequence=VSP_031844, VSP_031845;
CC Name=3;
CC IsoId=A3FIN4-3; Sequence=VSP_031846, VSP_031847;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:19657017}.
CC -!- DEVELOPMENTAL STAGE: Not detected in testis until 18 days postpartum.
CC At 22 days postpartum, levels increase and remain constant during
CC adulthood. During spermatogenesis, expressed from pachytene
CC spermatocytes to mature sperm. {ECO:0000269|PubMed:19657017}.
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; EF377342; ABN48718.1; -; mRNA.
DR EMBL; AK076708; BAC36451.1; -; mRNA.
DR EMBL; AK078567; BAC37336.1; -; mRNA.
DR EMBL; AL732504; CAM16526.1; -; Genomic_DNA.
DR EMBL; AL732504; CAM16528.2; -; Genomic_DNA.
DR CCDS; CCDS18091.2; -. [A3FIN4-1]
DR RefSeq; NP_796169.2; NM_177195.3. [A3FIN4-1]
DR AlphaFoldDB; A3FIN4; -.
DR SMR; A3FIN4; -.
DR STRING; 10090.ENSMUSP00000103575; -.
DR iPTMnet; A3FIN4; -.
DR PhosphoSitePlus; A3FIN4; -.
DR PaxDb; A3FIN4; -.
DR PRIDE; A3FIN4; -.
DR ProteomicsDB; 265156; -. [A3FIN4-1]
DR ProteomicsDB; 265157; -. [A3FIN4-2]
DR ProteomicsDB; 265158; -. [A3FIN4-3]
DR DNASU; 320571; -.
DR Ensembl; ENSMUST00000102953; ENSMUSP00000100018; ENSMUSG00000028457. [A3FIN4-2]
DR Ensembl; ENSMUST00000107942; ENSMUSP00000103575; ENSMUSG00000028457. [A3FIN4-1]
DR GeneID; 320571; -.
DR KEGG; mmu:320571; -.
DR UCSC; uc008spj.1; mouse. [A3FIN4-2]
DR UCSC; uc008spk.1; mouse. [A3FIN4-3]
DR UCSC; uc008spl.1; mouse. [A3FIN4-1]
DR CTD; 320571; -.
DR MGI; MGI:2444287; Atp8b5.
DR VEuPathDB; HostDB:ENSMUSG00000028457; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000161917; -.
DR HOGENOM; CLU_000846_3_2_1; -.
DR InParanoid; A3FIN4; -.
DR OMA; NDMERIM; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; A3FIN4; -.
DR TreeFam; TF300654; -.
DR BioGRID-ORCS; 320571; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Atp8b5; mouse.
DR PRO; PR:A3FIN4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A3FIN4; protein.
DR Bgee; ENSMUSG00000028457; Expressed in spermatocyte and 48 other tissues.
DR ExpressionAtlas; A3FIN4; baseline and differential.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
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:0140345; F:phosphatidylcholine flippase activity; IMP:UniProtKB.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IMP:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; IPR030350; FetA.
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:SF52; PTHR24092:SF52; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasmic vesicle; Lipid transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1183
FT /note="Phospholipid-transporting ATPase FetA"
FT /id="PRO_0000321955"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 904..924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 927..947
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1049..1069
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1090..1110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 416
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 838
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 842
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 304..305
FT /note="IF -> VS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031844"
FT VAR_SEQ 306..1183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031845"
FT VAR_SEQ 454..460
FT /note="KDKVDFS -> VSNYSFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031846"
FT VAR_SEQ 461..1183
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031847"
FT CONFLICT 2..33
FT /note="KYVKAFVSEISWDCSWYCSAMQERRNEDRQKE -> GSNGASSHRTSTLLTG
FT QPSQHPRLVSEQIPQQ (in Ref. 3; CAM16528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1183 AA; 135899 MW; AFB70541AE6A0714 CRC64;
MKYVKAFVSE ISWDCSWYCS AMQERRNEDR QKEEEERILQ ANNRRFNSLF EYPDNSIKTS
KYGFFNFLPM NLFEQFQRLA NAYFLILLFL QLVPQISSLA WYTTVIPLIV VLSITGVKDA
IDDVKRHRSD QQINNRSVSI LVNGRVEEIK WRNVQVGDII KLENNHPVTA DMLLLSSSEP
YGLTYIETAD LDGETNLKVK QAISVTSAME DNLELLSSFN GEVRCDPPNN KLDKFSGTLS
YLGNTYLLNH ERLLLRGCVI RNTDWCYGLV VYTGQDTKLM QNSGRSTFKR THIDHLMNVL
VVWIFMFLGG MCFLLSIGHG IWENSRGYYF QAFLPWKHYI TSSATSSALI FWSYFIVLNT
MVPISLYVSV EIIRLGNSYY INWDRKMFYA PKNMPAQART TTLNEELGQV QYVFSDKTGT
LTENVMIFNK CSINGKTYGY SYDDNGEYVP KSPKDKVDFS YNHLADPKFS FYDKTLVEAV
KSEDPLVYLF FLCLSLCHTV MSEEKVEGEL VYQAQSPDEG ALVTATRNFG FVFCSRTPET
ITVIEMGKIR VYRLLAILDF SNERKRMSVI VRTPEDRVML FCKGADTIIY ELLHPSCASL
SEVTMDHLDD FASEGLRTLM VAYRELDKAY FQTWIKKHGE AWLTLENRER KLALVYEEIE
RDLMLLGATA IEDKLQRGVP ETIVTLSKAK IKIWVLTGDK QETAVNIAYS CRIFKDEMDG
VFMVEGTDRE TVLEELRTAR KKMKPESLLE SDPINMYLAR KPKMPFKSLD EVANGNYGLV
ISGYSLAYAL EGSLEFELLR TACMCKGVVC CRMTPLQKAQ VVDLVKRYKK VVTLAIGDGA
NDISMIKAAH IGVGISNQEG MQATLSSDFS FCQFHFLQRL LLVHGRLSYN RMCKFLSYFF
YKNFAFTLVH FWYAFFNGFS AQTVYDIWFI TFYNLIYTSL PVLGLSLFEK DVNETWSLCY
PELYEPGQHN LYFNKKEFVK CLLHGIYNSF VLFFVPMGTV FNSERNDGKD ISDFQSFSLL
VQTTLIGVMT MQIALRTTSW TMINHTFTWG SLGLYFCILI LLCSDGLCLR YPSIFNFLGV
ARNSLSQPQI WLCLILSTIL CMIPLIGYNF LRPLLWPINA DKVLNRIHFC LKHPIPTQVQ
TKIKHPSLRR SAYAFSHKQG FGALITSGKT LKSSALAKSK RFL
