SCP1_MEDTR
ID SCP1_MEDTR Reviewed; 495 AA.
AC A0A0C3VJP4; A0A396ITK9; G7J647;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 3.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Serine carboxypeptidase 1 {ECO:0000303|PubMed:26511916};
DE EC=3.4.16.- {ECO:0000250|UniProtKB:P00729};
DE Flags: Precursor;
GN Name=SCP1 {ECO:0000303|PubMed:26511916};
GN OrderedLocusNames=MTR_3g079630 {ECO:0000312|EMBL:AES71591.2};
GN ORFNames=MtrunA17_Chr3g0118891 {ECO:0000312|EMBL:RHN68892.1};
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 [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 [2]
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 [3]
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).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH KPI106 AND KPI111, AND
RP TISSUE SPECIFICITY.
RX PubMed=23662629; DOI=10.1111/tpj.12242;
RA Rech S.S., Heidt S., Requena N.;
RT "A tandem Kunitz protease inhibitor (KPI106)-serine carboxypeptidase (SCP1)
RT controls mycorrhiza establishment and arbuscule development in Medicago
RT truncatula.";
RL Plant J. 75:711-725(2013).
RN [5]
RP INDUCTION BY RAM1 AND GLOMUS VERSIFORME.
RX PubMed=26511916; DOI=10.1104/pp.15.01155;
RA Park H.-J., Floss D.S., Levesque-Tremblay V., Bravo A., Harrison M.J.;
RT "Hyphal branching during arbuscule development requires reduced arbuscular
RT mycorrhiza1.";
RL Plant Physiol. 169:2774-2788(2015).
CC -!- FUNCTION: Carboxypeptidase that, together with KPI106, controls
CC mycorrhiza establishment and arbuscule development during root
CC colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus
CC irregularis). {ECO:0000269|PubMed:23662629}.
CC -!- SUBUNIT: Interacts with KPI106 and KPI111.
CC {ECO:0000269|PubMed:23662629}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted,
CC extracellular space, apoplast {ECO:0000269|PubMed:23662629}.
CC -!- INDUCTION: Accumulates in roots, in a RAM1-dependent manner, during
CC colonization by arbuscular mycorrhizal (AM) fungi (e.g. Glomus
CC versiforme). {ECO:0000269|PubMed:26511916}.
CC -!- DISRUPTION PHENOTYPE: Aberrant mycorrhizal development with an
CC increased number of septated hyphae and degenerate arbuscules during
CC root colonization by arbuscular mycorrhizal (AM) fungi (e.g.
CC Rhizophagus irregularis). {ECO:0000269|PubMed:23662629}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AES71591.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=RHN68892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM001219; AES71591.2; ALT_SEQ; Genomic_DNA.
DR EMBL; PSQE01000003; RHN68892.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003601340.2; XM_003601292.2.
DR AlphaFoldDB; A0A0C3VJP4; -.
DR SMR; A0A0C3VJP4; -.
DR MEROPS; S10.A41; -.
DR EnsemblPlants; AES71591; AES71591; MTR_3g079630.
DR Gramene; AES71591; AES71591; MTR_3g079630.
DR KEGG; mtr:MTR_3g079630; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_2_1; -.
DR OrthoDB; 84353at33090; -.
DR Proteomes; UP000002051; Chromosome 3.
DR Proteomes; UP000265566; Chromosome 3.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW Apoplast; Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..495
FT /note="Serine carboxypeptidase 1"
FT /id="PRO_5014483708"
FT ACT_SITE 226
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT ACT_SITE 414
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT ACT_SITE 465
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 133..377
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 294..305
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 329..349
FT /evidence="ECO:0000250|UniProtKB:P00729"
SQ SEQUENCE 495 AA; 55297 MW; F7A2E5824497F853 CRC64;
MEKVSLYACL ILNLSLLVIF PYSKASQADK LNEFILSRKS QNPPKTLSWE EGDALKTLFS
SAAYVAPPQE ELRLADKIVT LPGQPYGVNF DQYSGYVTVD PETGRELFYY FVESPCNSST
KPLVLWLNGG PGCSSLGYGA FQELGPFRVN SDGKTLYRNP YAWNEVANVL FLESPAGIGF
SYSNTTSDYD KSGDKSTAKD SYVFLINWLE RFPQYKTRDF YISGESYAGH YVPQLASTIL
HNNKLYKNTI INLKGISLGN AWIDDATSLK GLYDNLWTHA LNSDQTHELI EKYCDFTKQN
YSAICTNAMN MSMIEKGKID SFNIYAPLCH DSTLKNGSTG YVSNDLDPCS DYYGTAYLNR
PEVQKALHAK PTNWSHCSDS INLNWKDSPI TILPTIKYLI DNGIKLWIYS GDTDAVGVTI
SRYPINTLKL PIDSTWRPWY SGKEIGGYVV GYKGLTFVTV RGAGHLVPSW QPERALTLIS
SFLYGILPAS VSPSN
