SURO1_CAEEL
ID SURO1_CAEEL Reviewed; 664 AA.
AC Q9XU75;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Putative carboxypeptidase suro-1 {ECO:0000305};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q9UI42};
DE AltName: Full=Suppressor of roller 1 {ECO:0000312|WormBase:R11A5.7};
DE Flags: Precursor;
GN Name=suro-1 {ECO:0000312|WormBase:R11A5.7};
GN ORFNames=R11A5.7 {ECO:0000312|WormBase:R11A5.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ILE-110 AND GLY-407.
RX PubMed=21094156; DOI=10.1016/j.febslet.2010.11.020;
RA Kim T.H., Kim Y.J., Cho J.W., Shim J.;
RT "A novel zinc-carboxypeptidase SURO-1 regulates cuticle formation and body
RT morphogenesis in Caenorhabditis elegans.";
RL FEBS Lett. 585:121-127(2011).
CC -!- FUNCTION: May play a role in processing or organization of cuticle
CC collagen proteins, including rol-6 and col-19.
CC {ECO:0000269|PubMed:21094156}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15085};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:21094156}. Secreted {ECO:0000305|PubMed:21094156}.
CC -!- TISSUE SPECIFICITY: Localizes in stripes along the cuticle.
CC {ECO:0000269|PubMed:21094156}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the 3-fold embryonic stage to young
CC adult and at the larval stage in hypodermal and intestinal cells.
CC {ECO:0000269|PubMed:21094156}.
CC -!- DOMAIN: The ShKT and Thr-rich domains are required for body
CC morphogenesis. {ECO:0000269|PubMed:21094156}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a slightly
CC shorter and stouter body. {ECO:0000269|PubMed:21094156}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BX284601; CAB05602.2; -; Genomic_DNA.
DR PIR; T24170; T24170.
DR RefSeq; NP_492177.2; NM_059776.6.
DR AlphaFoldDB; Q9XU75; -.
DR SMR; Q9XU75; -.
DR STRING; 6239.R11A5.7; -.
DR MEROPS; M14.035; -.
DR EPD; Q9XU75; -.
DR PaxDb; Q9XU75; -.
DR PeptideAtlas; Q9XU75; -.
DR EnsemblMetazoa; R11A5.7.1; R11A5.7.1; WBGene00011235.
DR GeneID; 172557; -.
DR KEGG; cel:CELE_R11A5.7; -.
DR UCSC; R11A5.7.1; c. elegans.
DR CTD; 172557; -.
DR WormBase; R11A5.7; CE32478; WBGene00011235; suro-1.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_2_3_1; -.
DR InParanoid; Q9XU75; -.
DR OMA; RYLCKSI; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; Q9XU75; -.
DR PRO; PR:Q9XU75; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011235; Expressed in embryo and 3 other tissues.
DR GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR003582; ShKT_dom.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cytoplasmic vesicle; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..110
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436543"
FT CHAIN 111..664
FT /note="Putative carboxypeptidase suro-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004336700"
FT DOMAIN 621..657
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 512..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 437
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 219..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 306..307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 362..363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT DISULFID 621..657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 628..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 639..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT MUTAGEN 110
FT /note="I->F: In jg43; Abnormal localization of the collagen
FT proteins rol-6 and col-19."
FT /evidence="ECO:0000269|PubMed:21094156"
FT MUTAGEN 407
FT /note="G->E: In jg34; Shorter and stouter body. Abnormal
FT localization of the collagen proteins rol-6 and col-19. In
FT mutants lacking rol-6, suppresses body rolling and restores
FT normal orientation of alea."
FT /evidence="ECO:0000269|PubMed:21094156"
SQ SEQUENCE 664 AA; 75153 MW; A476FED3232739C5 CRC64;
MRYLCKSILL AVHTILLVGS VCCSTDVHNT DDKYALIHVS AHDEQSLHLI KQLQLNDFKY
DLDFWKSPSS ISDKADIMVK RGKSERMLRQ ILSFANVTVS MSVPDVEKLI MRNEGTTSKS
HLGFGSLSKW LHDDPILDSE PDLDLTKVGA LKKAKYPFGD YASYADMVKY MRTIEFYYPR
IAKIVRIGAT HEGKPIEGLK IGARSSHKKR AVWVDGNIHA REWASSHTAL YFINQLVSEY
GKDAQITNYV DTLDFYIVPC LNPDGYEYTR TSPIPTVRLW RKNRSPELCR PSLWGGEKCC
RGVDLNRNFR FHWAERGSSY EPCSNIYHGE EVFSEPETRA VRNFLATPEM KDRVDAFVTL
HSYAQLWIYP YSHEEQNYPE DIGELRKTAR KAINRLSRVY GTNYRMGTGA DTLSPAAGGS
DDWAKSALNV KYVYLIELRP QMELSNGFIL HKKELIPTAV ETFEGFREVV DAVLTLNNST
SSIGLSSGSN TSRKTISDLQ MRKQQYRMRL LASQAAGSTT RSTTTLKTST TSVSTTSEAT
SPSKTSRHFD RFTADLNSST RARPTPPMAP PIMSPSTEFS TTTTEEEDVT GVIRSSSIAS
RATTYGFFTA TKPSAFLDPE CRDMRYSCGF WLKNNKQVCE EQQSFMRAQC AYTCKFCTSF
IKRH
