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AQPA_DICDI
ID   AQPA_DICDI              Reviewed;         279 AA.
AC   Q9U8P7; Q55FK7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Aquaporin A;
GN   Name=aqpA; ORFNames=DDB_G0267378;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, FUNCTION, AND
RP   INDUCTION.
RC   STRAIN=AX4;
RX   PubMed=10876090; DOI=10.1016/s0378-1119(00)00201-8;
RA   Mitra B.N., Yoshino R., Morio T., Yokoyama M., Maeda M., Urushihara H.,
RA   Tanaka Y.;
RT   "Loss of a member of the aquaporin gene family, aqpA affects spore dormancy
RT   in Dictyostelium.";
RL   Gene 251:131-139(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX4;
RA   Mitra B.N., Yoshino R., Morio T., Urushihara H., Tanaka Y.;
RT   "Characterization of a water channel protein gene aqpA in Dictyostelium
RT   discoideum.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: May form a water-specific channel (By similarity). Required
CC       for prolonged spore survival on fruiting bodies. {ECO:0000250,
CC       ECO:0000269|PubMed:10876090}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: First detected at the tight mound stage. Highly
CC       expressed in fingers and late culminants. In slugs, detected in
CC       prespore cells, but not in prestalk cells.
CC       {ECO:0000269|PubMed:10876090}.
CC   -!- INDUCTION: Constitutively expressed during hyperosmotic stress.
CC       {ECO:0000269|PubMed:10876090}.
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). Here, the second motif is Asn-Pro-Val (NPV).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000305}.
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DR   EMBL; AB032841; BAA85158.1; -; Genomic_DNA.
DR   EMBL; AB008431; BAF94060.1; -; mRNA.
DR   EMBL; AAFI02000003; EAL73141.1; -; Genomic_DNA.
DR   RefSeq; XP_647526.1; XM_642434.1.
DR   AlphaFoldDB; Q9U8P7; -.
DR   SMR; Q9U8P7; -.
DR   STRING; 44689.DDB0191271; -.
DR   PaxDb; Q9U8P7; -.
DR   EnsemblProtists; EAL73141; EAL73141; DDB_G0267378.
DR   GeneID; 8616333; -.
DR   KEGG; ddi:DDB_G0267378; -.
DR   dictyBase; DDB_G0267378; aqpA.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_3_1; -.
DR   InParanoid; Q9U8P7; -.
DR   OMA; WTPGPLH; -.
DR   PhylomeDB; Q9U8P7; -.
DR   Reactome; R-DDI-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Reactome; R-DDI-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR   Reactome; R-DDI-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-DDI-432047; Passive transport by Aquaporins.
DR   PRO; PR:Q9U8P7; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR   GO; GO:0006833; P:water transport; IBA:GO_Central.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; PTHR19139; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..279
FT                   /note="Aquaporin A"
FT                   /id="PRO_0000327505"
FT   TOPO_DOM        1..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..69
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..114
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..158
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           96..98
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           214..216
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  29906 MW;  1B4928E57ACC7EA7 CRC64;
     MVKVVPLRFI TYDPLKDPSK MIYRRPISKP VKAFKGFFSE FLGTLYLVYF CGGSVCAAFA
     VAGDSAARAL LGGLIQGMAL AALIWAVSGV SGCNLNPAVT LANLLSGRVG LIDSLYYVAA
     QILGCIAGAG ILYGCLPNMY RIDLGVPHLA PGMNTGQAFL MEMMLTSILC LCVLGTSVFN
     VWDRRLNRIA PFAIGLALFI GVAIGFNFSG GALNPVRVLG PSIISGVWSH HWVYWLGPIV
     GAILAAFIYR CLLQERFDVI ERPGYIAPLI DPSTAVSSY
 
 
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