SCP37_ARATH
ID SCP37_ARATH Reviewed; 487 AA.
AC Q84WF0; Q9SV03;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine carboxypeptidase-like 37;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL37; OrderedLocusNames=At3g52010; ORFNames=F4F15.120;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-487.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=15908604; DOI=10.1104/pp.104.057950;
RA Fraser C.M., Rider L.W., Chapple C.;
RT "An expression and bioinformatics analysis of the Arabidopsis serine
RT carboxypeptidase-like gene family.";
RL Plant Physiol. 138:1136-1148(2005).
CC -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems,
CC flowers and siliques. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AL049711; CAB41321.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78874.1; -; Genomic_DNA.
DR EMBL; BT003902; AAO41950.1; -; mRNA.
DR PIR; T49080; T49080.
DR RefSeq; NP_190769.1; NM_115060.3.
DR AlphaFoldDB; Q84WF0; -.
DR SMR; Q84WF0; -.
DR ESTHER; arath-SCP37; Carboxypeptidase_S10.
DR MEROPS; S10.A31; -.
DR PaxDb; Q84WF0; -.
DR PRIDE; Q84WF0; -.
DR ProteomicsDB; 232770; -.
DR EnsemblPlants; AT3G52010.1; AT3G52010.1; AT3G52010.
DR GeneID; 824364; -.
DR Gramene; AT3G52010.1; AT3G52010.1; AT3G52010.
DR KEGG; ath:AT3G52010; -.
DR Araport; AT3G52010; -.
DR TAIR; locus:2083705; AT3G52010.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_2_1; -.
DR InParanoid; Q84WF0; -.
DR OMA; DTYNIYA; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q84WF0; -.
DR PRO; PR:Q84WF0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84WF0; baseline.
DR Genevisible; Q84WF0; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..487
FT /note="Serine carboxypeptidase-like 37"
FT /id="PRO_0000274652"
FT ACT_SITE 215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..368
FT /evidence="ECO:0000250"
FT DISULFID 280..291
FT /evidence="ECO:0000250"
FT DISULFID 315..336
FT /evidence="ECO:0000250"
SQ SEQUENCE 487 AA; 54915 MW; 536DFBB999870EC5 CRC64;
MVKQQDWSVT TCVLLFLFLA SQIHCRSGIH VSKRLEGSKQ GDGKSGDTSF NVLRRVLSPK
EKDLIKKLPG QPSGVSFRQY GGYVPVNEPS SRFLYYYFVE AIKPNTSTPL VIWFNGGPAC
SSLGGAFLEL GPFRVHSGGR KLFRNPYSWN NEANVLFLES PVTTGFSYSS NPIDLEELGE
KGDKATAEDN YIFLMNWLER FPEYKGRDIY IAGQSYAGHY VPQLAQIIIH RNKKTLVNLR
GILIGNPSLL TSIQDPYGYE FMLSHGLMSQ QQMDNYNQFC LRDDLYDNDK CALSVKTIDD
AKKHLDTYNI YAPVCLNSTL SRISKKCTTV LEVDPCSKDY LKAYLNRKKV QKAIHANTTK
LPYEWTSCNN ELTENWSEND RDTPMIPILH ELMGEGVRVM IYNGDVDLEI PFASTLAVVK
EMNLTVVKEF RPWFTGGQLG GFTEDYKGNL TFVTVKGAGH SVPTDQPIHA LNIFTSFIRN
TPLPHTA
