SCP44_ARATH
ID SCP44_ARATH Reviewed; 479 AA.
AC Q9MAR8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine carboxypeptidase-like 44;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL44; OrderedLocusNames=At1g43780; ORFNames=F28H19.3, F28H19.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC006423; AAF63101.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31996.1; -; Genomic_DNA.
DR PIR; G96501; G96501.
DR RefSeq; NP_175046.1; NM_103506.1.
DR AlphaFoldDB; Q9MAR8; -.
DR SMR; Q9MAR8; -.
DR ESTHER; arath-SCP44; Carboxypeptidase_S10.
DR MEROPS; S10.A25; -.
DR PaxDb; Q9MAR8; -.
DR PRIDE; Q9MAR8; -.
DR ProteomicsDB; 232962; -.
DR EnsemblPlants; AT1G43780.1; AT1G43780.1; AT1G43780.
DR GeneID; 840974; -.
DR Gramene; AT1G43780.1; AT1G43780.1; AT1G43780.
DR KEGG; ath:AT1G43780; -.
DR Araport; AT1G43780; -.
DR TAIR; locus:2029127; AT1G43780.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_1_1; -.
DR InParanoid; Q9MAR8; -.
DR OMA; KWRFLEV; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q9MAR8; -.
DR PRO; PR:Q9MAR8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAR8; baseline and differential.
DR Genevisible; Q9MAR8; 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; 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; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..479
FT /note="Serine carboxypeptidase-like 44"
FT /id="PRO_0000274659"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..352
FT /evidence="ECO:0000250"
FT DISULFID 253..270
FT /evidence="ECO:0000250"
FT DISULFID 295..320
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 53923 MW; 87A36BB1C46E1080 CRC64;
MVGGKWRFLE VAVVVMVLQW SCDYNGNLAE GFPVQDLVTK LPGQPEVAFR QFAGYVDIDV
KAGRSLFYYF VEAEKQPHSK PLTLWLNGGP GCSSIGGGAF TELGPFYPTG DARGLRRNPK
SWNKASNLLF VDSPAGVGWS YSNTTSDYTT GDESTAKDML VFMLRWLEKF PQFKTRNLFL
AGESYAGHYV PQLADVILEY NAQRSNRFKF NLKGIAIGNP LLKLDRDVPA IYEFFWSHGM
ISDELGLTIM NQCDFEDYTF TDSHNISKLC EAAVNQAGTI ITQYVNYYDI LLDVCYPSLF
EQELRLKKMG TRMSFGVDVC MSFEEQLYLN LPEVQKALHA NRTKLPYEWS MCSSLLNYKY
TDGNANMLPI LKRIVKSKVP VWVFSGDEDS VIPLLGSRTL VKELADDLNF NTTVPYGAWF
DKGQVGGWVV EYGNLLTFAT VRGAAHMVPY SQPSRALHLF TSFVLGRKLP HKSPPALHD
