AT135_HUMAN
ID AT135_HUMAN Reviewed; 1218 AA.
AC Q4VNC0; Q6UWS4; Q6ZWL0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable cation-transporting ATPase 13A5;
DE EC=7.2.2.-;
DE AltName: Full=P5-ATPase isoform 5;
GN Name=ATP13A5; ORFNames=UNQ488/PRO1004;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15925480; DOI=10.1016/j.ygeno.2005.04.002;
RA Kwasnicka-Crawford D.A., Carson A.R., Roberts W., Summers A.M.,
RA Rehnstrom K., Jarvela I., Scherer S.W.;
RT "Characterization of a novel cation transporter ATPase gene (ATP13A4)
RT interrupted by 3q25-q29 inversion in an individual with language delay.";
RL Genomics 86:182-194(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1016, AND VARIANT TYR-96.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1065-1218, AND VARIANT ALA-1131.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ89030.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ89030.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC85490.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AY823163; AAX24103.1; -; mRNA.
DR EMBL; AK122613; BAC85490.1; ALT_SEQ; mRNA.
DR EMBL; AY358667; AAQ89030.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33914.1; -.
DR RefSeq; NP_940907.2; NM_198505.2.
DR AlphaFoldDB; Q4VNC0; -.
DR SMR; Q4VNC0; -.
DR STRING; 9606.ENSP00000341942; -.
DR GlyGen; Q4VNC0; 3 sites.
DR iPTMnet; Q4VNC0; -.
DR PhosphoSitePlus; Q4VNC0; -.
DR BioMuta; ATP13A5; -.
DR DMDM; 74753861; -.
DR MassIVE; Q4VNC0; -.
DR PaxDb; Q4VNC0; -.
DR PeptideAtlas; Q4VNC0; -.
DR PRIDE; Q4VNC0; -.
DR ProteomicsDB; 62310; -.
DR Antibodypedia; 65947; 10 antibodies from 6 providers.
DR DNASU; 344905; -.
DR Ensembl; ENST00000342358.9; ENSP00000341942.4; ENSG00000187527.12.
DR GeneID; 344905; -.
DR KEGG; hsa:344905; -.
DR MANE-Select; ENST00000342358.9; ENSP00000341942.4; NM_198505.4; NP_940907.2.
DR UCSC; uc011bsq.3; human.
DR CTD; 344905; -.
DR DisGeNET; 344905; -.
DR GeneCards; ATP13A5; -.
DR HGNC; HGNC:31789; ATP13A5.
DR HPA; ENSG00000187527; Group enriched (breast, choroid plexus, salivary gland).
DR MIM; 619119; gene.
DR neXtProt; NX_Q4VNC0; -.
DR OpenTargets; ENSG00000187527; -.
DR PharmGKB; PA134952038; -.
DR VEuPathDB; HostDB:ENSG00000187527; -.
DR eggNOG; KOG0208; Eukaryota.
DR GeneTree; ENSGT00940000160327; -.
DR HOGENOM; CLU_001828_0_0_1; -.
DR InParanoid; Q4VNC0; -.
DR OMA; KMEDCNV; -.
DR OrthoDB; 172453at2759; -.
DR PhylomeDB; Q4VNC0; -.
DR TreeFam; TF300331; -.
DR PathwayCommons; Q4VNC0; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 344905; 10 hits in 1061 CRISPR screens.
DR GenomeRNAi; 344905; -.
DR Pharos; Q4VNC0; Tdark.
DR PRO; PR:Q4VNC0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q4VNC0; protein.
DR Bgee; ENSG00000187527; Expressed in nasal cavity epithelium and 87 other tissues.
DR ExpressionAtlas; Q4VNC0; baseline and differential.
DR Genevisible; Q4VNC0; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 cation transmembrane transporter activity; IBA:GO_Central.
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:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF12409; P5-ATPase; 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; TIGR01494; ATPase_P-type; 1.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1218
FT /note="Probable cation-transporting ATPase 13A5"
FT /id="PRO_0000337122"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1042..1062
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1077..1097
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1115..1135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 486
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 850
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 854
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 96
FT /note="S -> Y (in dbSNP:rs12637558)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061039"
FT VARIANT 133
FT /note="E -> Q (in dbSNP:rs6797429)"
FT /id="VAR_043614"
FT VARIANT 739
FT /note="G -> S (in dbSNP:rs2280268)"
FT /id="VAR_043615"
FT VARIANT 1053
FT /note="I -> V (in dbSNP:rs6787746)"
FT /id="VAR_043616"
FT VARIANT 1131
FT /note="V -> A (in dbSNP:rs2271791)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_043617"
FT VARIANT 1204
FT /note="K -> Q (in dbSNP:rs7428010)"
FT /id="VAR_043618"
FT CONFLICT 357
FT /note="K -> E (in Ref. 2; BAC85490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1218 AA; 137327 MW; 70A58A83549DEE31 CRC64;
MEENSKKDHR ALLNQGEEDE LEVFGYRDHN VRKAFCLVAS VLTCGGLLLV FYWRPQWRVW
ANCIPCPLQE ADTVLLRTTD EFQRYMRKKV FCLYLSTLKF PVSKKWEESL VADRHSVINQ
ALIKPELKLR CMEVQKIRYV WNDLEKRFQK VGLLEDSNSC SDIHQTFGLG LTSEEQEVRR
LVCGPNAIEV EIQPIWKLLV KQVLNPFYVF QAFTLTLWLS QGYIEYSVAI IILTVISIVL
SVYDLRQQSV KLHNLVEDHN KVQVTIIVKD KGLEELESRL LVPGDILILP GKFSLPCDAV
LIDGSCVVNE GMLTGESIPV TKTPLPQMEN TMPWKCHSLE DYRKHVLFCG TEVIQVKPSG
QGPVRAVVLQ TGYNTAKGDL VRSILYPRPL NFKLYSDAFK FIVFLACLGV MGFFYALGVY
MYHGVPPKDT VTMALILLTV TVPPVLPAAL TIGNVYAQKR LKKKKIFCIS PQRINMCGQI
NLVCFDKTGT LTEDGLDLWG TVPTADNCFQ EAHSFASGQA VPWSPLCAAM ASCHSLILLN
GTIQGDPLDL KMFEGTAWKM EDCIVDSCKF GTSVSNIIKP GPKASKSPVE AIITLCQFPF
SSSLQRMSVI AQLAGENHFH VYMKGAPEMV ARFCRSETVP KNFPQELRSY TVQGFRVIAL
AHKTLKMGNL SEVEHLAREK VESELTFLGL LIMENRLKKE TKLVLKELSE ARIRTVMITG
DNLQTAITVA KNSEMIPPGS QVIIVEADEP EEFVPASVTW QLVENQETGP GKKEIYMHTG
NSSTPRGEGG SCYHFAMSGK SYQVIFQHFN SLLPKILVNG TVFARMSPGQ KSSLIEEFQK
LNYYVGMCGD GANDCGALKA AHAGISLSEQ EASVASPFTS KTTNIQCVPH LIREGRAALV
SSFGVFKYLT MYGIIQFISA LLLYWQLQLF GNYQYLMQDV AITLMVCLTM SSTHAYPKLA
PYRPAGQLLS PPLLLSIFLN SCFSCIVQIS AFLYVKQQPW YCEVYQYSEC FLANQSNFST
NVSLERNWTG NATLIPGSIL SFETTTLWPI TTINYITVAF IFSKGKPFRK PIYTNYIFSF
LLLAALGLTI FILFSDFQVI YRGMELIPTI TSWRVLILVV ALTQFCVAFF VEDSILQNHE
LWLLIKREFG FYSKSQYRTW QKKLAEDSTW PPINRTDYSG DGKNGFYING GYESHEQIPK
RKLKLGGQPT EQHFWARL
