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
//