ID AT134_CHICK Reviewed; 1204 AA.
AC Q5ZKB7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 117.
DE RecName: Full=Probable cation-transporting ATPase 13A4;
DE EC=7.2.2.-;
DE AltName: Full=P5-ATPase isoform 4;
GN Name=ATP13A4; ORFNames=RCJMB04_11o9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; AJ720167; CAG31826.1; -; mRNA.
DR RefSeq; NP_001026485.1; NM_001031314.1.
DR AlphaFoldDB; Q5ZKB7; -.
DR SMR; Q5ZKB7; -.
DR STRING; 9031.ENSGALP00000011610; -.
DR PaxDb; 9031-ENSGALP00000011610; -.
DR GeneID; 424901; -.
DR KEGG; gga:424901; -.
DR CTD; 84239; -.
DR VEuPathDB; HostDB:geneid_424901; -.
DR eggNOG; KOG0208; Eukaryota.
DR InParanoid; Q5ZKB7; -.
DR PhylomeDB; Q5ZKB7; -.
DR PRO; PR:Q5ZKB7; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; 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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR GO; GO:0015203; F:polyamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:1902047; P:polyamine transmembrane transport; IBA:GO_Central.
DR CDD; cd07542; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
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 SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 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 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1204
FT /note="Probable cation-transporting ATPase 13A4"
FT /id="PRO_0000318677"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..897
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..929
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 968..988
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 989..1043
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1044..1064
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1065..1075
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1076..1096
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1097..1113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1114..1134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1135..1204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 483
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 845
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1204 AA; 134058 MW; B6AECD6FE30FFDEB CRC64;
MGENPAKSHY AQLNLGEENE MEIFGYKTQC CRKALCIAGY ILSCGALLLL FYWKPEWDVW
ANCVPCSLEE ADVVLLRTTD EFRIYSRKNV TWISVSGIIK SRLDYPSFAE EDSIFSKALM
KPSLQVKSIQ VQKIRYVWNI YAKQFQKVGA LEDHHTCSAI HTKFGSGLTC SEQSLRRVIC
GPNTIDVPVI PIWKLLIKEV LNPFYVFQLF SVCLWFAEDY MEYAAAIIIM SPLSISLTVY
DLRQQSVKLQ RLVESHNSIM VTGRNKEGFQ ELESHHLVPG DMVVLKEGKA LLPCDAILIS
GQCIVNESML TGESIPVTKT QLPQADNLKP WKMHCAEDYK KHVLFCGTEV IQTKGDDRGV
VKAVVLQTGF NTAKGDLVRS ILYPKPMNFR LYRDALRFLM CLIAFAAIGM IYTVCVFALN
GEEAGEVVKK ALDVITIAVP PALPAALTTG IIYTQRRLKK KGIFCISPQR INMCGQLNLI
CFDKTGTLTE DGLDLWGLLP SEGNCFQDVR RFPADHSLPW GPAFRAMVVC HSLIVLEGKI
QGDPLDVKMF EATNWVIDDS SGHQIEGQRS THATVIRPGP KANTASVDGI TILHQFPFSS
ALQRMSVIAQ ETGGEKQAFT KGAPEMVATL CRAETVPSNF ESKLLFYTAQ GFRVIGLAYK
SLQSGKQSTD LTREEVESDL TFLGLLIMEN RLKRETKPVL EELSAAHIRS VMVTGDNIQT
AVTVAKNAGM ISPTNRVILV EANKIPGSFS ASVTWKPLKE NKTEDDGNLD SGSQTGRRIR
LAAEPGQFHF AMSGKSYQVV AQYFSHLLPK LLLNATVFAR MSPSQKSSLV EEFQKLDYFV
GMCGDGANDC GALKVAHAGI SLSEQEASVA SPFTSRTPSI ACVPELIREG RAALVTSFCM
FKYMALYSTI QYLGVLLLYW QLNSFGNYQF LFQDLAITTV IGMTMSFTEA YPKLVPYRPP
SQLVSPPLLL SVILNILFSL GMQILGFLMV QKQPWYSKTD IHSACLSVNN HVENSSSASS
LGLHGVGGGD PTEVDNGYKS YENTTVWLLS TINCLIIALV FSKGKPFRQP IYTNYVFIMV
LVGQLGVCLF LVFADIDDLY SKMDLVCTPT TWRISMVMML AVTLAVSFLV EEAIIENRAL
WLWLKKTFQY HSKSHYKRLQ RVLEQDSAWP PLNETFSLDA VTVSVEEDME GHSNPTFDSN
EDAL
//
