UBA5_CHICK
ID UBA5_CHICK Reviewed; 397 AA.
AC Q6IVA4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000305};
DE Short=Ubiquitin-activating enzyme 5 {ECO:0000250|UniProtKB:Q9GZZ9};
DE AltName: Full=UFM1-activating enzyme {ECO:0000305};
DE AltName: Full=Ubiquitin activating enzyme-like protein {ECO:0000303|Ref.1};
GN Name=UBA5 {ECO:0000250|UniProtKB:Q9GZZ9};
GN Synonyms=UBAL {ECO:0000303|Ref.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xue P., Chen W., Zhang J., Ci H.L., Li Y.P.;
RT "Expression pattern of UBAL in embryo development.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1-like enzyme which specifically catalyzes the first step in
CC ufmylation. Activates UFM1 by first adenylating its C-terminal glycine
CC residue with ATP, and thereafter linking this residue to the side chain
CC of a cysteine residue in E1, yielding a UFM1-E1 thioester and free AMP.
CC Activates UFM1 via a trans-binding mechanism, in which UFM1 interacts
CC with distinct sites in both subunits of the UBA5 homodimer. Trans-
CC binding also promotes stabilization of the UBA5 homodimer, and enhances
CC ATP-binding. Transfer of UFM1 from UBA5 to the E2-like enzyme UFC1 also
CC takes place using a trans mechanism. Ufmylation is involved in
CC reticulophagy (also called ER-phagy) induced in response to endoplasmic
CC reticulum stress. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SUBUNIT: Homodimer; homodimerization is required for UFM1 activation.
CC Interacts (via UIS motif) with UFM1; binds UFM1 via a trans-binding
CC mechanism in which UFM1 interacts with distinct sites in both subunits
CC of the UBA5 homodimer. Interacts (via C-terminus) with UFC1.
CC {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9GZZ9}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9GZZ9}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000305}.
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DR EMBL; AY620963; AAT39515.1; -; mRNA.
DR RefSeq; NP_001001765.1; NM_001001765.1.
DR AlphaFoldDB; Q6IVA4; -.
DR SMR; Q6IVA4; -.
DR STRING; 9031.ENSGALP00000019110; -.
DR PaxDb; Q6IVA4; -.
DR GeneID; 414879; -.
DR KEGG; gga:414879; -.
DR CTD; 79876; -.
DR VEuPathDB; HostDB:geneid_414879; -.
DR eggNOG; KOG2336; Eukaryota.
DR InParanoid; Q6IVA4; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; Q6IVA4; -.
DR PRO; PR:Q6IVA4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030219; P:megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0071569; P:protein ufmylation; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; ISS:UniProtKB.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..397
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391932"
FT MOTIF 327..339
FT /note="UFM1-interacting sequence (UIS)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT ACT_SITE 243
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
SQ SEQUENCE 397 AA; 44178 MW; E82183A7A53D3AA4 CRC64;
MAERVELLER RVRELERELE LARGGRASAR ARIETMSPEV TDSNPYSRLM ALKRMGIVKD
YEKIRTFTVA IVGVGGVGSV TAEMLTRCGI GKLLLFDYDK VELANMNRLF FQPHQAGLSK
VQAAEHTLRN INPDVQFEVH NYNITTLDNF EHFMDRISNG ALEEGKPVDL VLSCVDNFEA
RMAINTACNE LGQIWMESGV SENAVSGHIQ LIIPGESACF ACAPPLVVAA NIDEKTLKRE
GVCAASLPTT MGVVAGILVQ NVLKYLLNFG TVSYYLGYNA MQDFFPTMAM KPNPQCSDQN
CRKQQENYKI KEAAQPKQEE IHQEEEIVHE DNDWGIELVS ETTEDELKAA SGPVPDLPVG
ITVAYTIPNK EENLTAEETV AESEESLEDL MAKMRNL
