ID   AQP12_MOUSE             Reviewed;         290 AA.
AC   Q8CHJ2; Q3KNM4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Aquaporin-12;
DE            Short=AQP-12;
GN   Name=Aqp12;
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], AND TISSUE SPECIFICITY.
RX   PubMed=15809071; DOI=10.1016/j.bbrc.2005.03.046;
RA   Itoh T., Rai T., Kuwahara M., Ko S.B., Uchida S., Sasaki S., Ishibashi K.;
RT   "Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 330:832-838(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC       neutral solutes across cell membranes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Restricted to pancreatic acinar cells.
CC       {ECO:0000269|PubMed:15809071}.
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC       membrane-spanning domains and a pore-forming loop with the signature
CC       motif Asn-Pro-Ala (NPA).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB084104; BAC45227.1; -; mRNA.
DR   EMBL; BC107213; AAI07214.1; -; mRNA.
DR   CCDS; CCDS15183.1; -.
DR   RefSeq; NP_808255.1; NM_177587.2.
DR   AlphaFoldDB; Q8CHJ2; -.
DR   SMR; Q8CHJ2; -.
DR   STRING; 10090.ENSMUSP00000060622; -.
DR   iPTMnet; Q8CHJ2; -.
DR   PhosphoSitePlus; Q8CHJ2; -.
DR   PaxDb; Q8CHJ2; -.
DR   PRIDE; Q8CHJ2; -.
DR   ProteomicsDB; 265078; -.
DR   Ensembl; ENSMUST00000059676; ENSMUSP00000060622; ENSMUSG00000045091.
DR   GeneID; 208760; -.
DR   KEGG; mmu:208760; -.
DR   UCSC; uc007cdc.2; mouse.
DR   CTD; 208760; -.
DR   MGI; MGI:2664636; Aqp12.
DR   VEuPathDB; HostDB:ENSMUSG00000045091; -.
DR   eggNOG; ENOG502RYFD; Eukaryota.
DR   GeneTree; ENSGT00530000063816; -.
DR   HOGENOM; CLU_074449_3_0_1; -.
DR   InParanoid; Q8CHJ2; -.
DR   OMA; YFQKTRF; -.
DR   OrthoDB; 1080106at2759; -.
DR   PhylomeDB; Q8CHJ2; -.
DR   TreeFam; TF320251; -.
DR   Reactome; R-MMU-432047; Passive transport by Aquaporins.
DR   BioGRID-ORCS; 208760; 0 hits in 71 CRISPR screens.
DR   PRO; PR:Q8CHJ2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8CHJ2; protein.
DR   Bgee; ENSMUSG00000045091; Expressed in pancreas and 11 other tissues.
DR   Genevisible; Q8CHJ2; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015267; F:channel activity; IBA:GO_Central.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR016697; Aquaporin_11/12.
DR   InterPro; IPR023265; Aquaporin_12.
DR   InterPro; IPR000425; MIP.
DR   PANTHER; PTHR21191:SF8; PTHR21191:SF8; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PIRSF; PIRSF017529; Aquaporin_11/12; 1.
DR   PRINTS; PR02025; AQUAPORIN12.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..290
FT                   /note="Aquaporin-12"
FT                   /id="PRO_0000063972"
FT   TRANSMEM        1..21
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..138
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REGION          271..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           93..95
FT                   /note="NPA 1"
FT   MOTIF           212..214
FT                   /note="NPA 2"
SQ   SEQUENCE   290 AA;  31290 MW;  2945B01824429C63 CRC64;
     MASLNVSLCF FFATCAICEV ARRASKALLP AGTYASFARG AVGAAQLAAC CLEMRVLVEL
     GPWAGGFGPD LLLTLVFLLF LVHGVTFDGA SANPTVALQE FLMVEASLPN TLLKLSAQVL
     GAQAACALTQ RCWAWELSEL HLLQSLMAAH CSSTLRTSVL QGMLVEGACT FFFHLSLLHL
     QHSLLVYRVP ALALLVTLMA YTAGPYTSAF FNPALAASVT FHCPGNTLLE YAHVYCLGPV
     AGMILAVLLH QGHLPRLFQR NLFYRQKSKY RTPRGKLSPG SVDAKMHKGE