ID   NO26_SOYBN              Reviewed;         271 AA.
AC   P08995;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Nodulin-26;
DE            Short=N-26;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Evans;
RX   PubMed=3174457; DOI=10.1093/nar/16.19.9347;
RA   Sandal N.N., Marcker K.A.;
RT   "Soybean nodulin 26 is homologous to the major intrinsic protein of the
RT   bovine lens fiber membrane.";
RL   Nucleic Acids Res. 16:9347-9347(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 67-271.
RC   STRAIN=cv. Prize;
RX   PubMed=3822816; DOI=10.1093/nar/15.2.813;
RA   Fortin M.G., Morrison N.A., Verma D.P.S.;
RT   "Nodulin-26, a peribacteroid membrane nodulin is expressed independently of
RT   the development of the peribacteroid compartment.";
RL   Nucleic Acids Res. 15:813-824(1987).
RN   [3]
RP   SEQUENCE REVISION TO 184 AND 257.
RA   Miao G.H.;
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION AT SER-262 BY CPK.
RX   PubMed=1390682; DOI=10.1021/bi00152a035;
RA   Waever C.D., Roberts D.M.;
RT   "Determination of the site of phosphorylation of nodulin 26 by the calcium-
RT   dependent protein kinase from soybean nodules.";
RL   Biochemistry 31:8954-8959(1992).
CC   -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC       neutral solutes across cell membranes. This aquaporin may function in
CC       transporting small molecules across the peribacteroid membranes.
CC   -!- SUBCELLULAR LOCATION: Symbiosome, peribacteroid membrane; Multi-pass
CC       membrane protein.
CC   -!- INDUCTION: During nodulation in legume roots after Rhizobium infection.
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. NIP (TC
CC       1.A.8.12) subfamily. {ECO:0000305}.
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DR   EMBL; X04782; CAA28471.1; -; mRNA.
DR   EMBL; X12659; CAA31186.1; -; mRNA.
DR   PIR; JQ2286; JQ2286.
DR   PIR; S01444; S01444.
DR   RefSeq; NP_001235870.1; NM_001248941.1.
DR   AlphaFoldDB; P08995; -.
DR   SMR; P08995; -.
DR   STRING; 3847.GLYMA08G12650.1; -.
DR   TCDB; 1.A.8.12.1; the major intrinsic protein (mip) family.
DR   iPTMnet; P08995; -.
DR   GeneID; 547904; -.
DR   KEGG; gmx:547904; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   OrthoDB; 1152704at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043661; C:peribacteroid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
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; PTHR45724; PTHR45724; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   1: Evidence at protein level;
KW   Membrane; Nodulation; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..271
FT                   /note="Nodulin-26"
FT                   /id="PRO_0000064071"
FT   TRANSMEM        40..62
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..94
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..137
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..174
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..203
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..247
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           97..99
FT                   /note="NPA 1"
FT   MOTIF           209..211
FT                   /note="NPA 2"
FT   MOD_RES         262
FT                   /note="Phosphoserine; by CPK"
FT                   /evidence="ECO:0000269|PubMed:1390682"
SQ   SEQUENCE   271 AA;  28936 MW;  EA323421D39042B4 CRC64;
     MADYSAGTES QEVVVNVTKN TSETIQRSDS LVSVPFLQKL VAEAVGTYFL IFAGCASLVV
     NENYYNMITF PGIAIVWGLV LTVLVYTVGH ISGGHFNPAV TIAFASTRRF PLIQVPAYVV
     AQLLGSILAS GTLRLLFMGN HDQFSGTVPN GTNLQAFVFE FIMTFFLMFV ICGVATDNRA
     VGEFAGIAIG STLLLNVIIG GPVTGASMNP ARSLGPAFVH GEYEGIWIYL LAPVVGAIAG
     AWVYNIVRYT DKPLSETTKS ASFLKGRAAS K