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UFM1_CHICK
ID   UFM1_CHICK              Reviewed;          85 AA.
AC   Q5ZMK7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000250|UniProtKB:P61960};
DE   Flags: Precursor;
GN   Name=UFM1 {ECO:0000250|UniProtKB:P61960};
GN   ORFNames=RCJMB04_1l24 {ECO:0000303|PubMed:15642098};
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 [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Ubiquitin-like modifier which can be covalently attached via
CC       an isopeptide bond to lysine residues of substrate proteins as a
CC       monomer or a lysine-linked polymer. The so-called ufmylation, requires
CC       the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme
CC       UFC1, and the UFM1-ligase E3 enzyme UFL1. Ufmylation is involved in
CC       reticulophagy (also called ER-phagy) induced in response to endoplasmic
CC       reticulum stress. {ECO:0000250|UniProtKB:P61960}.
CC   -!- SUBUNIT: Interacts with UBA5. Interacts with UFC1.
CC       {ECO:0000250|UniProtKB:P61960}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61960}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P61960}.
CC   -!- SIMILARITY: Belongs to the UFM1 family. {ECO:0000305}.
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DR   EMBL; AJ719377; CAG31036.1; -; mRNA.
DR   RefSeq; NP_001025998.1; NM_001030827.1.
DR   AlphaFoldDB; Q5ZMK7; -.
DR   SMR; Q5ZMK7; -.
DR   STRING; 9031.ENSGALP00000027483; -.
DR   PaxDb; Q5ZMK7; -.
DR   Ensembl; ENSGALT00000049545; ENSGALP00000043924; ENSGALG00000017042.
DR   GeneID; 418894; -.
DR   KEGG; gga:418894; -.
DR   CTD; 51569; -.
DR   VEuPathDB; HostDB:geneid_418894; -.
DR   eggNOG; KOG3483; Eukaryota.
DR   GeneTree; ENSGT00390000010391; -.
DR   HOGENOM; CLU_175114_0_0_1; -.
DR   InParanoid; Q5ZMK7; -.
DR   OMA; INPAQNA; -.
DR   OrthoDB; 1575050at2759; -.
DR   PhylomeDB; Q5ZMK7; -.
DR   TreeFam; TF312934; -.
DR   PRO; PR:Q5ZMK7; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000017042; Expressed in colon and 14 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
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; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR005375; UFM1.
DR   PANTHER; PTHR15825; PTHR15825; 1.
DR   Pfam; PF03671; Ufm1; 1.
DR   PIRSF; PIRSF038027; Ubiquitin-like_Ufm1; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..83
FT                   /note="Ubiquitin-fold modifier 1"
FT                   /id="PRO_0000042132"
FT   PROPEP          84..85
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT                   /id="PRO_0000042133"
FT   CROSSLNK        69
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in UFM1)"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT   CROSSLNK        83
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
SQ   SEQUENCE   85 AA;  9087 MW;  E5CDADAB5A55DD7B CRC64;
     MSKVTFKVTL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
     QTAGNVFLKH GSDLRIIPRD RVGSS
 
 
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