CPC_CUCSA
ID CPC_CUCSA Reviewed; 137 AA.
AC P29602;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cucumber peeling cupredoxin;
DE Short=CPC;
DE AltName: Full=Stellacyanin;
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND HYDROXYLATION AT
RP PRO-115; PRO-116; PRO-117; PRO-121; PRO-122; PRO-127; PRO-128; PRO-129;
RP PRO-133; PRO-134 AND PRO-136.
RC TISSUE=Peelings;
RX PubMed=1468551; DOI=10.1016/0014-5793(92)81475-2;
RA Mann K., Schaefer W., Thoenes U., Messerschmidt A., Mehrabian Z.,
RA Nalbandyan R.;
RT "The amino acid sequence of a type I copper protein with an unusual
RT serine- and hydroxyproline-rich C-terminal domain isolated from cucumber
RT peelings.";
RL FEBS Lett. 314:220-223(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), DISULFIDE BOND, AND METAL-BINDING
RP SITES HIS-46; CYS-89; HIS-94 AND GLN-99.
RX PubMed=8931136; DOI=10.1002/pro.5560051104;
RA Hart P.J., Nersissian A.M., Herrmann R.G., Nalbandyan R.M., Valentine J.S.,
RA Eisenberg D.;
RT "A missing link in cupredoxins: crystal structure of cucumber stellacyanin
RT at 1.6-A resolution.";
RL Protein Sci. 5:2175-2183(1996).
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 PIR; S27034; SSKV.
DR PDB; 1JER; X-ray; 1.60 A; A=1-137.
DR PDBsum; 1JER; -.
DR AlphaFoldDB; P29602; -.
DR SMR; P29602; -.
DR STRING; 3659.XP_004163544.1; -.
DR EnsemblPlants; KGN45265; KGN45265; Csa_7G432470.
DR Gramene; KGN45265; KGN45265; Csa_7G432470.
DR EvolutionaryTrace; P29602; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR039391; Phytocyanin.
DR InterPro; IPR003245; Phytocyanin_dom.
DR PANTHER; PTHR33021; PTHR33021; 1.
DR Pfam; PF02298; Cu_bind_like; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
DR PROSITE; PS51485; PHYTOCYANIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Electron transport; Glycoprotein; Hydroxylation; Metal-binding;
KW Pyrrolidone carboxylic acid; Transport.
FT CHAIN 1..137
FT /note="Cucumber peeling cupredoxin"
FT /id="PRO_0000085553"
FT DOMAIN 3..107
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT REGION 112..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 89
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 94
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 99
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 115
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 116
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 117
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 121
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 122
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 127
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 128
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 129
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 133
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 134
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT MOD_RES 136
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1468551"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 60..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818,
FT ECO:0000269|PubMed:8931136"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1JER"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1JER"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:1JER"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1JER"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1JER"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1JER"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:1JER"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1JER"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1JER"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1JER"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1JER"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1JER"
SQ SEQUENCE 137 AA; 14747 MW; F15FBCB5CB34A8CB CRC64;
QSTVHIVGDN TGWSVPSSPN FYSQWAAGKT FRVGDSLQFN FPANAHNVHE METKQSFDAC
NFVNSDNDVE RTSPVIERLD ELGMHYFVCT VGTHCSNGQK LSINVVAANA TVSMPPPSSS
PPSSVMPPPV MPPPSPS
