LOCUS       NP_036957                323 aa            linear   ROD 18-MAR-2025
DEFINITION  aquaporin-4 isoform M1 [Rattus norvegicus].
ACCESSION   NP_036957
VERSION     NP_036957.1
DBSOURCE    REFSEQ: accession NM_012825.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Chen,K., Xu,B., Qiu,S., Long,L., Zhao,Q., Xu,J. and Wang,H.
  TITLE     Inhibition of phosphodiesterase 4 attenuates aquaporin 4 expression
            and astrocyte swelling following cerebral ischemia/reperfusion
            injury
  JOURNAL   Glia 72 (9), 1629-1645 (2024)
   PUBMED   38785370
  REMARK    GeneRIF: Inhibition of phosphodiesterase 4 attenuates aquaporin 4
            expression and astrocyte swelling following cerebral
            ischemia/reperfusion injury.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Chen,Z., Liu,B., Zhou,D., Lei,M., Yang,J., Hu,Z. and Duan,W.
  TITLE     AQP4 regulates ferroptosis and oxidative stress of Muller cells in
            diabetic retinopathy by regulating TRPV4
  JOURNAL   Exp Cell Res 439 (1), 114087 (2024)
   PUBMED   38735619
  REMARK    GeneRIF: AQP4 regulates ferroptosis and oxidative stress of Muller
            cells in diabetic retinopathy by regulating TRPV4.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Pisani,F., Rossi,A., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational regulation mechanisms of aquaporin-4 supramolecular
            organization in astrocytes
  JOURNAL   Glia 59 (12), 1923-1932 (2011)
   PUBMED   21850708
  REMARK    GeneRIF: When transfected in Hela cells, the longer rat AQP4
            isoform, not present in humans, impairs formation of the orthogonal
            array of particles in astrocyte primary cultures.
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Hirt,B., Gleiser,C., Eckhard,A., Mack,A.F., Muller,M., Wolburg,H.
            and Lowenheim,H.
  TITLE     All functional aquaporin-4 isoforms are expressed in the rat
            cochlea and contribute to the formation of orthogonal arrays of
            particles
  JOURNAL   Neuroscience 189, 79-92 (2011)
   PUBMED   21621589
  REMARK    GeneRIF: Identified all functional AQP4 isoforms -M1, M23, and Mz-
            and the formation of higher-order complexes in the organ of Corti
            of the rat.
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Moe,S.E., Sorbo,J.G., Sogaard,R., Zeuthen,T., Petter Ottersen,O.
            and Holen,T.
  TITLE     New isoforms of rat Aquaporin-4
  JOURNAL   Genomics 91 (4), 367-377 (2008)
   PUBMED   18255256
  REMARK    GeneRIF: rat AQP4 has six cDNA isoforms, formed by alternative
            splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond
            to the two classical M1 and M23 isoforms, respectively
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Jung,J.S., Bhat,R.V., Preston,G.M., Guggino,W.B., Baraban,J.M. and
            Agre,P.
  TITLE     Molecular characterization of an aquaporin cDNA from brain:
            candidate osmoreceptor and regulator of water balance
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 13052-13056 (1994)
   PUBMED   7528931
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000018.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene. A
            recent study provided evidence for translational readthrough in
            this gene and expression of an additional C-terminally extended
            isoform via the use of an alternative in-frame translation
            termination codon. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1, also known as AQP4a)
            represents the predominant transcript and encodes two isoforms,
            which result from the use of alternative in-frame translation
            termination codons. The shorter isoform (M1) results from
            translation termination at the upstream UGA stop codon, while the
            longer isoform (M1x) results from UGA stop codon readthrough to the
            downstream UAA termination codon. This RefSeq represents the
            shorter isoform (M1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.72618.1,
                                           SRR26643429.53390.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            regulatory uORF        :: PMID: 21850708
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..323
                     /product="aquaporin-4 isoform M1"
                     /note="mercurial-insensitive water channel"
                     /calculated_mol_wt=34349
     Region          23
                     /region_name="alternative AUG translation initiation site"
     Region          31..248
                     /region_name="MIP"
                     /note="Major intrinsic protein; pfam00230"
                     /db_xref="CDD:395174"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            70..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            order(77,95..97,209..210,213,216)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(97..99,213..215)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     Region          97..99
                     /region_name="NPA 1.
                     /evidence=ECO:0000305|PubMed:16325200,
                     ECO:0000305|PubMed:19406128"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG.
                     /evidence=ECO:0000250|UniProtKB:P55088; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:19800950; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Region          213..215
                     /region_name="NPA 2.
                     /evidence=ECO:0000305|PubMed:16325200,
                     ECO:0000305|PubMed:19406128"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12692561,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P55088; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     CDS             1..323
                     /gene="Aqp4"
                     /gene_synonym="AQP-4; Miwc; WCH4"
                     /coded_by="NM_012825.4:67..1038"
                     /note="isoform M1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25293"
                     /db_xref="RGD:2143"
ORIGIN      
        1 msdgaaarrw gkcgppcsre simvafkgvw tqafwkavta eflamlifvl lsvgstinwg
       61 gsenplpvdm vlislcfgls iatmvqcfgh isgghinpav tvamvctrki siaksvfyit
      121 aqclgaiiga gilylvtpps vvgglgvttv hgnltaghgl lveliitfql vftifascds
      181 krtdvtgsva laigfsvaig hlfainytga smnparsfgp avimgnwenh wiywvgpiig
      241 avlagalyey vfcpdvelkr rlkeafskaa qqtkgsymev ednrsqvete dlilkpgvvh
      301 vididrgdek kgkdssgevl ssv
//
