SBP_SOYBN
ID SBP_SOYBN Reviewed; 524 AA.
AC Q04672;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Sucrose-binding protein;
DE Short=SBP;
DE Flags: Precursor;
GN Name=SBP;
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], AND PROTEIN SEQUENCE OF 30-50.
RC TISSUE=Embryo;
RX PubMed=1467654; DOI=10.2307/3869499;
RA Grimes H.D., Overvoorde P.J., Ripp K., Franceschi V.R., Hitz W.D.;
RT "A 62-kD sucrose binding protein is expressed and localized in tissues
RT actively engaged in sucrose transport.";
RL Plant Cell 4:1561-1574(1992).
CC -!- FUNCTION: Plays a role in sucrose transport.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Associated with the plasma membrane of several cell
CC types engaged in sucrose transport, including the mesophyll cells of
CC young sink leaves, the companion cells of mature phloem and the cells
CC of developing cotyledons.
CC -!- DEVELOPMENTAL STAGE: In the cotyledon, expression is not detected until
CC 10 days after fertilization. Between 10-19 days after fertilization,
CC expression increases rapidly but declines 20-30 days after
CC fertilization. 30 days after fertilization, no expression occurs. This
CC expression pattern closely parallels the rate of sucrose uptake in the
CC cotyledon.
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DR EMBL; L06038; AAB03894.1; -; mRNA.
DR PIR; JQ1730; JQ1730.
DR RefSeq; NP_001276308.1; NM_001289379.1.
DR AlphaFoldDB; Q04672; -.
DR SMR; Q04672; -.
DR STRING; 3847.GLYMA10G03390.1; -.
DR PRIDE; Q04672; -.
DR GeneID; 100787186; -.
DR KEGG; gmx:100787186; -.
DR eggNOG; ENOG502QQEP; Eukaryota.
DR InParanoid; Q04672; -.
DR OrthoDB; 1072107at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000326; C:protein storage vacuole; IEA:UniProt.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Reference proteome; Signal;
KW Sugar transport; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:1467654"
FT CHAIN 30..524
FT /note="Sucrose-binding protein"
FT /id="PRO_0000022282"
FT DOMAIN 110..271
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 312..478
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 73..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 60523 MW; 0251EE90796EF341 CRC64;
MGMRTKLSLA IFFFFLLALF SNLAFGKCKE TEVEEEDPEL VTCKHQCQQQ QQYTEGDKRV
CLQSCDRYHR MKQEREKQIQ EETREKKEEE SREREEEQQE QHEEQDENPY IFEEDKDFET
RVETEGGRIR VLKKFTEKSK LLQGIENFRL AILEARAHTF VSPRHFDSEV VFFNIKGRAV
LGLVSESETE KITLEPGDMI HIPAGTPLYI VNRDENDKLF LAMLHIPVSV STPGKFEEFF
APGGRDPESV LSAFSWNVLQ AALQTPKGKL ENVFDQQNEG SIFRISREQV RALAPTKKSS
WWPFGGESKP QFNIFSKRPT ISNGYGRLTE VGPDDDEKSW LQRLNLMLTF TNITQRSMST
IHYNSHATKI ALVIDGRGHL QISCPHMSSR SSHSKHDKSS PSYHRISSDL KPGMVFVVPP
GHPFVTIASN KENLLMICFE VNARDNKKFT FAGKDNIVSS LDNVAKELAF NYPSEMVNGV
FLLQRFLERK LIGRLYHLPH KDRKESFFFP FELPREERGR RADA