UFSP_CAEEL
ID UFSP_CAEEL Reviewed; 589 AA.
AC Q94218; Q86MF8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ufm1-specific protease {ECO:0000250|UniProtKB:Q9NUQ7};
DE Short=UfSP {ECO:0000250|UniProtKB:Q9NUQ7};
DE EC=3.4.22.- {ECO:0000269|PubMed:29251776};
DE AltName: Full=Odorant response abnormal protein 8 {ECO:0000303|PubMed:9590179};
GN Name=odr-8 {ECO:0000303|PubMed:9590179, ECO:0000312|WormBase:F38A5.1a};
GN Synonyms=ufsp-2 {ECO:0000312|WormBase:F38A5.1a};
GN ORFNames=F38A5.1 {ECO:0000312|WormBase:F38A5.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9590179; DOI=10.1016/s0092-8674(00)81173-3;
RA Dwyer N.D., Troemel E.R., Sengupta P., Bargmann C.I.;
RT "Odorant receptor localization to olfactory cilia is mediated by ODR-4, a
RT novel membrane-associated protein.";
RL Cell 93:455-466(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12410303; DOI=10.1038/nature01169;
RA de Bono M., Tobin D.M., Davis M.W., Avery L., Bargmann C.I.;
RT "Social feeding in Caenorhabditis elegans is induced by neurons that detect
RT aversive stimuli.";
RL Nature 419:899-903(2002).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23449979; DOI=10.1074/jbc.m113.458000;
RA Hertel P., Daniel J., Stegehake D., Vaupel H., Kailayangiri S., Gruel C.,
RA Woltersdorf C., Liebau E.;
RT "The ubiquitin-fold modifier 1 (Ufm1) cascade of Caenorhabditis elegans.";
RL J. Biol. Chem. 288:10661-10671(2013).
RN [5]
RP FUNCTION, INTERACTION WITH ODR-4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-421 AND HIS-547.
RX PubMed=24603482; DOI=10.1371/journal.pgen.1004082;
RA Chen C., Itakura E., Weber K.P., Hegde R.S., de Bono M.;
RT "An ER complex of ODR-4 and ODR-8/Ufm1 specific protease 2 promotes GPCR
RT maturation by a Ufm1-independent mechanism.";
RL PLoS Genet. 10:E1004082-E1004082(2014).
RN [6] {ECO:0007744|PDB:5XDA}
RP X-RAY CRYSTALLOGRAPHY (3.29 ANGSTROMS) OF 25-589 IN COMPLEX WITH UFM-1,
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-409; CYS-421; ASP-458;
RP TRP-469; ARG-488; HIS-547 AND ASN-578.
RX PubMed=29251776; DOI=10.1002/1873-3468.12951;
RA Kim K.H., Ha B.H., Kim E.E.;
RT "Structural basis for Ufm1 recognition by UfSP.";
RL FEBS Lett. 592:263-273(2018).
CC -!- FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide
CC bond at the C-terminal Gly of ufm-1, a ubiquitin-like modifier protein
CC bound to a number of target proteins (PubMed:29251776,
CC PubMed:24603482). Required, with oct-4, for the localization of a
CC subset of 7 transmembrane domain odorant receptors, including odr-10,
CC to the cilia of olfactory neurons AWA and AWC (PubMed:9590179).
CC Operates in aggregation behavior, and responses to oxygen levels
CC (PubMed:12410303). {ECO:0000269|PubMed:12410303,
CC ECO:0000269|PubMed:24603482, ECO:0000269|PubMed:29251776,
CC ECO:0000269|PubMed:9590179}.
CC -!- SUBUNIT: Interacts with odr-4. {ECO:0000269|PubMed:24603482}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23449979, ECO:0000269|PubMed:24603482}; Peripheral
CC membrane protein {ECO:0000269|PubMed:24603482}. Cytoplasm
CC {ECO:0000269|PubMed:24603482}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:23449979}. Note=Recruited to the endoplasmic
CC reticulum upon interaction with odr-4. {ECO:0000269|PubMed:24603482}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q94218-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q94218-2; Sequence=VSP_023644;
CC -!- TISSUE SPECIFICITY: Expressed in head and tail neurons
CC (PubMed:24603482). Expressed in the amphid head neurons ADL, ASI, ASH,
CC ASJ, ASG, ADF, ASK, AWA, AWB, AWC, and in two tail neurons, the phasmid
CC tail neurons PHA and PHB (PubMed:23449979).
CC {ECO:0000269|PubMed:23449979, ECO:0000269|PubMed:24603482}.
CC -!- DISRUPTION PHENOTYPE: Aberrant localization of odr-10, str-2, str-112
CC and str-113. Reduced response to odorants mediated by AWA and AWC
CC olfactory neurons. Increased aggregation and response to O2 levels when
CC knocked down with npr-1. {ECO:0000269|PubMed:12410303,
CC ECO:0000269|PubMed:24603482, ECO:0000269|PubMed:9590179}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. {ECO:0000305}.
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DR EMBL; FO080844; CCD67166.1; -; Genomic_DNA.
DR EMBL; FO080844; CCD67167.1; -; Genomic_DNA.
DR PIR; T29897; T29897.
DR RefSeq; NP_001023188.1; NM_001028017.2. [Q94218-1]
DR RefSeq; NP_001023189.1; NM_001028018.1. [Q94218-2]
DR PDB; 5EJJ; X-ray; 2.80 A; A/B=26-589.
DR PDB; 5XDA; X-ray; 3.29 A; A/B/C/D/E/F=25-589.
DR PDBsum; 5EJJ; -.
DR PDBsum; 5XDA; -.
DR AlphaFoldDB; Q94218; -.
DR SMR; Q94218; -.
DR BioGRID; 42538; 5.
DR STRING; 6239.F38A5.1a; -.
DR MEROPS; C78.A03; -.
DR EPD; Q94218; -.
DR PaxDb; Q94218; -.
DR PeptideAtlas; Q94218; -.
DR EnsemblMetazoa; F38A5.1a.1; F38A5.1a.1; WBGene00018160. [Q94218-1]
DR EnsemblMetazoa; F38A5.1b.1; F38A5.1b.1; WBGene00018160. [Q94218-2]
DR GeneID; 177417; -.
DR KEGG; cel:CELE_F38A5.1; -.
DR UCSC; F38A5.1a; c. elegans. [Q94218-1]
DR CTD; 177417; -.
DR WormBase; F38A5.1a; CE10028; WBGene00018160; odr-8. [Q94218-1]
DR WormBase; F38A5.1b; CE33641; WBGene00018160; odr-8. [Q94218-2]
DR eggNOG; KOG2433; Eukaryota.
DR GeneTree; ENSGT00940000157115; -.
DR InParanoid; Q94218; -.
DR OMA; VFLPAGW; -.
DR OrthoDB; 390107at2759; -.
DR PRO; PR:Q94218; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00018160; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:WormBase.
DR GO; GO:0071567; F:deUFMylase activity; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:WormBase.
DR GO; GO:0097499; P:protein localization to non-motile cilium; IMP:WormBase.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IGI:WormBase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR Pfam; PF07910; Peptidase_C78; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chemotaxis; Cytoplasm;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..589
FT /note="Ufm1-specific protease"
FT /id="PRO_0000280370"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /evidence="ECO:0000305|PubMed:29251776"
FT ACT_SITE 545
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT ACT_SITE 547
FT /evidence="ECO:0000305|PubMed:29251776"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_023644"
FT MUTAGEN 409
FT /note="Y->H: Strongly reduced ability to hydrolyze ufm-1
FT bound to a target protein."
FT /evidence="ECO:0000269|PubMed:29251776"
FT MUTAGEN 421
FT /note="C->A: No significant effect on GPCR localization in
FT AWA cilia."
FT /evidence="ECO:0000269|PubMed:24603482"
FT MUTAGEN 421
FT /note="C->S: Abolished ability to hydrolyze ufm-1 bound to
FT a target protein. No significant effect on GPCR
FT localization in AWA cilia or odorant chemotaxis."
FT /evidence="ECO:0000269|PubMed:24603482,
FT ECO:0000269|PubMed:29251776"
FT MUTAGEN 458
FT /note="D->A: Strongly reduced ability to hydrolyze ufm-1
FT bound to a target protein."
FT /evidence="ECO:0000269|PubMed:29251776"
FT MUTAGEN 469
FT /note="W->A: Strongly reduced ability to hydrolyze ufm-1
FT bound to a target protein."
FT /evidence="ECO:0000269|PubMed:29251776"
FT MUTAGEN 488
FT /note="R->A: Reduced ability to hydrolyze ufm-1 bound to a
FT target protein."
FT /evidence="ECO:0000269|PubMed:29251776"
FT MUTAGEN 547
FT /note="H->A: Abolished ability to hydrolyze ufm-1 bound to
FT a target protein. No significant effect on GPCR
FT localization in AWA cilia or odorant chemotaxis."
FT /evidence="ECO:0000269|PubMed:24603482,
FT ECO:0000269|PubMed:29251776"
FT MUTAGEN 578
FT /note="N->A: Strongly reduced ability to hydrolyze ufm-1
FT bound to a target protein."
FT /evidence="ECO:0000269|PubMed:29251776"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5XDA"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 151..164
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 260..272
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 278..305
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5XDA"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 446..450
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:5XDA"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5XDA"
FT HELIX 472..482
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 502..509
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 524..532
FT /evidence="ECO:0007829|PDB:5EJJ"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:5EJJ"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:5EJJ"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:5XDA"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:5EJJ"
SQ SEQUENCE 589 AA; 66581 MW; 4C74D5EE237704A4 CRC64;
MTNSQTVSLI GPTQMAPQST PPPPVNELWF IDAQAMFQNY ANLRSFSKSN ANEINTTIGG
FVFGRKARKQ VIHVLFAYAE DLTESNRQFL ESSLSADIEL VGNLNIDGQS QILPGGQFTL
QLTSRMLENR SISEFLDMNV MFNNEHVLME GASCVSRVGY EWSLRAGREQ EDVKSAAERL
SMASFRFTYL NAEHGLVIRE QKPEAAQQKY LDKFSKGAVP YKDVIEFTAM QSLTRDTSND
TEDQKLVPTV KVTKDNKHFT RLVTIGEVVF PAFFGDSSLD LYKRSREAFN RRANNTMMVT
VNGIRAGRGV TTTTSATYLP PGWVSLLHLQ LPTKWTDNEQ RNYRIRLHKL FNLPSSKPVL
RLSQALALHS ESARLTNKKL IREPHLSITN YQPVGEITTV NGPYNYHHYM QDGIDDSGWG
CAYRSFQTIW SWFILNGYTD KPVPSHREIQ QALVDIQDKQ AKFVGSRQWI GSTEISFVLN
ELLKLECRFI ATNSGAEVVE RVRELARHFE TSGTPVMIGG NMLAHTILGV DFNDTTGETK
FLVLDPHYTG SEDIKTITSK GWCAWKPASF WSKDHFYNMV LPQPPSDAI
