CYTM_SOLTU
ID CYTM_SOLTU Reviewed; 756 AA.
AC P37842;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Multicystatin;
DE Short=MC;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Superior;
RX PubMed=8251633; DOI=10.1007/bf00021535;
RA Waldron C., Wegrich L.M., Merlo P.A., Walsh T.A.;
RT "Characterization of a genomic sequence coding for potato multicystatin, an
RT eight-domain cysteine proteinase inhibitor.";
RL Plant Mol. Biol. 23:801-812(1993).
CC -!- FUNCTION: Probably has a role in the plant's defense system.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in tuber and leaf.
CC -!- INDUCTION: By wounding.
CC -!- SIMILARITY: Belongs to the cystatin family. Phytocystatin subfamily.
CC {ECO:0000305}.
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DR EMBL; L16450; AAA16120.1; -; Genomic_DNA.
DR PIR; S40305; S40305.
DR PDB; 2W9P; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=100-186.
DR PDB; 2W9Q; X-ray; 2.50 A; A=100-186.
DR PDB; 4LZI; X-ray; 2.20 A; A=380-660.
DR PDBsum; 2W9P; -.
DR PDBsum; 2W9Q; -.
DR PDBsum; 4LZI; -.
DR AlphaFoldDB; P37842; -.
DR SMR; P37842; -.
DR MEROPS; I25.015; -.
DR MEROPS; I25.034; -.
DR MEROPS; I25.036; -.
DR MEROPS; I25.039; -.
DR MEROPS; I25.040; -.
DR PRIDE; P37842; -.
DR EvolutionaryTrace; P37842; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P37842; baseline and differential.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR CDD; cd00042; CY; 8.
DR InterPro; IPR027214; Cystatin.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR PANTHER; PTHR11413; PTHR11413; 8.
DR Pfam; PF00031; Cystatin; 8.
DR SMART; SM00043; CY; 8.
DR SUPFAM; SSF54403; SSF54403; 8.
DR PROSITE; PS00287; CYSTATIN; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Protease inhibitor; Reference proteome; Repeat;
KW Thiol protease inhibitor.
FT CHAIN 1..756
FT /note="Multicystatin"
FT /id="PRO_0000207159"
FT DOMAIN 3..96
FT /note="Cystatin 1"
FT DOMAIN 97..191
FT /note="Cystatin 2"
FT DOMAIN 192..285
FT /note="Cystatin 3"
FT DOMAIN 286..380
FT /note="Cystatin 4"
FT DOMAIN 381..474
FT /note="Cystatin 5"
FT DOMAIN 475..568
FT /note="Cystatin 6"
FT DOMAIN 569..662
FT /note="Cystatin 7"
FT DOMAIN 663..756
FT /note="Cystatin 8"
FT MOTIF 48..52
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT MOTIF 142..146
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT MOTIF 237..241
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT MOTIF 331..335
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT MOTIF 426..430
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT MOTIF 520..524
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT MOTIF 614..618
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT MOTIF 708..712
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT SITE 5
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT SITE 99
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT SITE 194
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT SITE 288
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT SITE 383
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT SITE 477
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT SITE 571
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT SITE 665
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:2W9Q"
FT STRAND 131..157
FT /evidence="ECO:0007829|PDB:2W9Q"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2W9Q"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:2W9Q"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2W9Q"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:2W9Q"
FT HELIX 394..411
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 426..443
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 445..455
FT /evidence="ECO:0007829|PDB:4LZI"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 460..473
FT /evidence="ECO:0007829|PDB:4LZI"
FT HELIX 488..504
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 510..535
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 538..549
FT /evidence="ECO:0007829|PDB:4LZI"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 554..565
FT /evidence="ECO:0007829|PDB:4LZI"
FT HELIX 582..599
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 604..629
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 632..643
FT /evidence="ECO:0007829|PDB:4LZI"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:4LZI"
FT STRAND 648..658
FT /evidence="ECO:0007829|PDB:4LZI"
SQ SEQUENCE 756 AA; 86786 MW; 5F48D05CA921CD84 CRC64;
MAIVGGLVDV PFENKVEFDD LARFAVQDYN QKNDSSLEFK KVLNVKQQIV AGIMYYITFE
ATEGGNKKEY EAKILLRKWE DLKKVVGFKL VGDDSTMPGG IVNVPNPNNT KFQELARFAI
QDYNKKQNAH LEFVENLNVK EQVVAGIMYY ITLAATDDAG KKKIYKAKIW VKEWEDFKKV
VEFKLVGDDI AKLGGITDVP FPNNPEFQDL ARFAIQVYNK KENVHLEFVE NLNVKQQVVA
GMMYYITLAA IDAGKKKIYE TKIWVKEWED FKKVVEFKLV GDDSAKTGGI INVPNPNSPE
FQDLARFAVQ DYNNTQNAHL EFVENLNVKE QLVSGMMYYI TLAATDAGNK KEYEAKIWVK
EWEDFKKVID FKLVGNDSAK KLGGFTEVPF PNSPEFQDLT RFAVHQYNKD QNAHLEFVEN
LNVKKQVVAG MLYYITFAAT DGGKKKIYET KIWVKVWENF KKVVEFKLVG DDSAKLGGII
NVPFPNNPEF QDLARFAVQD YNKKENAHLE FVENLNVKEQ LVAGMLYYIT LVAIDAGKKK
IYEAKIWVKE WENFKKVIEF KLIGDDSAII GGFTDVPFPN NPEFQDLARF AVQDYNKKEN
AHLEYVENLN VKEQLVAGMI YYITLVATDA GKKKIYEAKI WVKEWEDFKK VVEFKLVGDD
SAKPGGIIIV PFPNSPEFQD LARFAVQDFN KKENGHLEFV ENLNVKEQVV AGMMYYITLA
ATDARKKEIY ETKILVKEWE NFKEVQEFKL VGDATK
