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Aquaporin-6 (AQP-6) (Aquaporin-2-like) (Kidney-specific aquaporin) (hKID)

 AQP6_HUMAN              Reviewed;         282 AA.
Q13520;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
05-DEC-2018, entry version 154.
RecName: Full=Aquaporin-6;
Short=AQP-6;
AltName: Full=Aquaporin-2-like;
AltName: Full=Kidney-specific aquaporin;
Short=hKID;
Name=AQP6; Synonyms=AQP2L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=8812490; DOI=10.1006/geno.1996.0396;
Ma T., Yang B., Kuo W.L., Verkman A.S.;
"cDNA cloning and gene structure of a novel water channel expressed
exclusively in human kidney: evidence for a gene cluster of aquaporins
at chromosome locus 12q13.";
Genomics 35:543-550(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
-!- FUNCTION: Forms a water-specific channel that participates in
distinct physiological functions such as glomerular filtration,
tubular endocytosis and acid-base metabolism. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA).
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
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EMBL; U48408; AAB41566.1; -; mRNA.
EMBL; AC025154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS31798.1; -.
RefSeq; NP_001643.2; NM_001652.3.
UniGene; Hs.54505; -.
PDB; 1S6E; Model; -; A=1-282.
PDBsum; 1S6E; -.
ProteinModelPortal; Q13520; -.
SMR; Q13520; -.
IntAct; Q13520; 244.
STRING; 9606.ENSP00000320247; -.
TCDB; 1.A.8.8.4; the major intrinsic protein (mip) family.
iPTMnet; Q13520; -.
PhosphoSitePlus; Q13520; -.
BioMuta; AQP6; -.
DMDM; 212276421; -.
PaxDb; Q13520; -.
PRIDE; Q13520; -.
ProteomicsDB; 59516; -.
Ensembl; ENST00000315520; ENSP00000320247; ENSG00000086159.
Ensembl; ENST00000615425; ENSP00000477688; ENSG00000086159.
GeneID; 363; -.
KEGG; hsa:363; -.
UCSC; uc001rvr.2; human.
CTD; 363; -.
DisGeNET; 363; -.
EuPathDB; HostDB:ENSG00000086159.12; -.
GeneCards; AQP6; -.
HGNC; HGNC:639; AQP6.
HPA; HPA015278; -.
MIM; 601383; gene.
neXtProt; NX_Q13520; -.
OpenTargets; ENSG00000086159; -.
PharmGKB; PA24924; -.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00940000161949; -.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; Q13520; -.
KO; K09868; -.
OMA; VHWVFWV; -.
OrthoDB; EOG091G166T; -.
PhylomeDB; Q13520; -.
TreeFam; TF312940; -.
Reactome; R-HSA-432047; Passive transport by Aquaporins.
GeneWiki; AQP6; -.
GenomeRNAi; 363; -.
PRO; PR:Q13520; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000086159; Expressed in 122 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_AQP6; -.
ExpressionAtlas; Q13520; baseline and differential.
Genevisible; Q13520; HS.
GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0015112; F:nitrate transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015250; F:water channel activity; IBA:GO_Central.
GO; GO:0007588; P:excretion; TAS:ProtInc.
GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR023254; Aquaporin_6.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
PANTHER; PTHR19139:SF113; PTHR19139:SF113; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR02018; AQUAPORIN6.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
2: Evidence at transcript level;
3D-structure; Complete proteome; Cytoplasmic vesicle; Membrane;
Polymorphism; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 282 Aquaporin-6.
/FTId=PRO_0000063955.
TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.
TRANSMEM 31 48 Helical. {ECO:0000255}.
TOPO_DOM 49 54 Extracellular. {ECO:0000255}.
TRANSMEM 55 73 Helical. {ECO:0000255}.
TOPO_DOM 74 99 Cytoplasmic. {ECO:0000255}.
TRANSMEM 100 121 Helical. {ECO:0000255}.
TOPO_DOM 122 141 Extracellular. {ECO:0000255}.
TRANSMEM 142 162 Helical. {ECO:0000255}.
TOPO_DOM 163 168 Cytoplasmic. {ECO:0000255}.
TRANSMEM 169 188 Helical. {ECO:0000255}.
TOPO_DOM 189 214 Extracellular. {ECO:0000255}.
TRANSMEM 215 236 Helical. {ECO:0000255}.
TOPO_DOM 237 282 Cytoplasmic. {ECO:0000255}.
MOTIF 82 84 NPA 1.
MOTIF 196 198 NPA 2.
VARIANT 234 234 V -> I (in dbSNP:rs17124220).
/FTId=VAR_047233.
CONFLICT 4 5 VE -> EV (in Ref. 1; AAB41566).
{ECO:0000305}.
CONFLICT 76 76 A -> T (in Ref. 1; AAB41566).
{ECO:0000305}.
CONFLICT 180 180 V -> W (in Ref. 1; AAB41566).
{ECO:0000305}.
CONFLICT 189 189 H -> L (in Ref. 1; AAB41566).
{ECO:0000305}.
CONFLICT 260 260 G -> R (in Ref. 1; AAB41566).
{ECO:0000305}.
SEQUENCE 282 AA; 29370 MW; BDA1B3DFCA5C685E CRC64;
MDAVEPGGRG WASMLACRLW KAISRALFAE FLATGLYVFF GVGSVMRWPT ALPSVLQIAI
TFNLVTAMAV QVTWKASGAH ANPAVTLAFL VGSHISLPRA VAYVAAQLVG ATVGAALLYG
VMPGDIRETL GINVVRNSVS TGQAVAVELL LTLQLVLCVF ASTDSRQTSG SPATMIGISV
ALGHLIGIHF TGCSMNPARS FGPAIIIGKF TVHWVFWVGP LMGALLASLI YNFVLFPDTK
TLAQRLAILT GTVEVGTGAG AGAEPLKKES QPGSGAVEME SV


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