VPYL_MEDTR
ID VPYL_MEDTR Reviewed; 464 AA.
AC D3J163;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Protein VAPYRIN-LIKE {ECO:0000303|PubMed:19912567};
DE Short=MtVpyl {ECO:0000303|PubMed:19912567};
GN Name=VPYL {ECO:0000303|PubMed:19912567};
GN OrderedLocusNames=MTR_1g089180 {ECO:0000312|EMBL:AES61829.1};
GN ORFNames=MtrunA17_Chr1g0196261 {ECO:0000312|EMBL:RHN81180.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=19912567; DOI=10.1111/j.1365-313x.2009.04072.x;
RA Pumplin N., Mondo S.J., Topp S., Starker C.G., Gantt J.S., Harrison M.J.;
RT "Medicago truncatula Vapyrin is a novel protein required for arbuscular
RT mycorrhizal symbiosis.";
RL Plant J. 61:482-494(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
CC -!- FUNCTION: May be involved in arbuscular mycorrhizal (AM) symbiosis with
CC AM fungi and in nitrogen-fixing rhizobial bacteria symbiosis leading to
CC the formation of root nodules. {ECO:0000250|UniProtKB:D3J162}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3J162}. Nucleus
CC {ECO:0000250|UniProtKB:D3J162}. Cell membrane
CC {ECO:0000250|UniProtKB:D3J162}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:19912567}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ423210; ADC33496.1; -; mRNA.
DR EMBL; CM001217; AES61829.1; -; Genomic_DNA.
DR EMBL; PSQE01000001; RHN81180.1; -; Genomic_DNA.
DR RefSeq; XP_003591578.1; XM_003591530.2.
DR AlphaFoldDB; D3J163; -.
DR SMR; D3J163; -.
DR STRING; 3880.AES61829; -.
DR EnsemblPlants; AES61829; AES61829; MTR_1g089180.
DR GeneID; 11415982; -.
DR Gramene; AES61829; AES61829; MTR_1g089180.
DR KEGG; mtr:MTR_1g089180; -.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_000134_53_1_1; -.
DR OMA; PGPHVFR; -.
DR OrthoDB; 672459at2759; -.
DR Proteomes; UP000002051; Chromosome 1.
DR Proteomes; UP000265566; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR Pfam; PF12796; Ank_2; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF49354; SSF49354; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50202; MSP; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..464
FT /note="Protein VAPYRIN-LIKE"
FT /id="PRO_0000450030"
FT DOMAIN 3..124
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REPEAT 153..182
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 186..215
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 217..246
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 252..281
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 285..314
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 318..347
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 349..368
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 372..401
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 405..435
FT /note="ANK 9"
FT /evidence="ECO:0000255"
SQ SEQUENCE 464 AA; 51003 MW; B413F2912083CF5A CRC64;
MDRLVKTEFN EVNLNFQKNQ KCSSSFKLTN LMHTMSVAVS LTTTNPTTFS INKPLSVIPP
LSSSTYTLHL TNLNQPPLSE PADVITVRTS MLPTGKATTD DLRRLFNKPG PHVFRDAVIT
VILVGPTVAE YVISNYETRN LFTKAISVCT KSNLTNLMKP AVESGKVEYV TDLITAGGDV
NFRDSNGKSL IPFAIRTGKL AVLKLLVANG CRINDSVDFV LHEAAIIDRV DVVKFLFESF
CDELDVNSVN REMMTPIHVS ASEGHVSLIE FFVSIGGNAN AVDSRRWTPL HHAASRNHLK
AVEFLLENSD VKYARELNGK TAFEIASESG HTRLFGVLRW GDALLQAARV DDVHALKKCL
GEGAEVNRKD QNGWTPLHWA SFKGRIKSVK VLLEHGAEVD SVDDAGYTPL HCAAEAGHLQ
VALVLIAHGG CQTNLKSFQH VSPIATFQKH VSLHYSTKKS ETFA