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ARL1_RAT
ID   ARL1_RAT                Reviewed;         181 AA.
AC   P61212; P41276;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=ADP-ribosylation factor-like protein 1;
GN   Name=Arl1; Synonyms=Arf7;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
RX   PubMed=8195219; DOI=10.1016/s0021-9258(17)40735-6;
RA   Schuermann A., Breiner M., Becker W., Huppertz C., Kaninulainen H.,
RA   Kentrup H., Joost H.-G.;
RT   "Cloning of two novel ADP-ribosylation factor-like proteins and
RT   characterization of their differential expression in 3T3-L1 cells.";
RL   J. Biol. Chem. 269:15683-15688(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   Lowe S.L., Hong W.J.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF GLY-2; THR-31 AND GLN-71.
RX   PubMed=11792819; DOI=10.1242/jcs.114.24.4543;
RA   Lu L., Horstmann H., Ng C., Hong W.;
RT   "Regulation of Golgi structure and function by ARF-like protein 1 (Arl1).";
RL   J. Cell Sci. 114:4543-4555(2001).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GOLGA1 AND GOLGA4.
RX   PubMed=12972563; DOI=10.1091/mbc.e03-01-0864;
RA   Lu L., Hong W.;
RT   "Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97
RT   and Golgin-245/p230 onto the Golgi.";
RL   Mol. Biol. Cell 14:3767-3781(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 16-180 IN COMPLEX WITH GDPNP;
RP   MAGNESIUM AND GOLGA4.
RX   PubMed=14718928; DOI=10.1038/nsmb714;
RA   Wu M., Lu L., Hong W., Song H.;
RT   "Structural basis for recruitment of GRIP domain golgin-245 by small GTPase
RT   Arl1.";
RL   Nat. Struct. Mol. Biol. 11:86-94(2004).
CC   -!- FUNCTION: GTP-binding protein. Can activate phospholipase D with very
CC       low efficiency (By similarity). Important for normal function of the
CC       Golgi apparatus. {ECO:0000250, ECO:0000269|PubMed:11792819,
CC       ECO:0000269|PubMed:12972563}.
CC   -!- SUBUNIT: The GTP-bound form interacts with RGPD8 (By similarity). The
CC       GTP-bound form directly interacts with ARFIP2; this interaction leads
CC       to an increase in the amount of bound GTP at steady state level (By
CC       similarity). Binds to SCOC, preferentially in its GTP-bound form. May
CC       interact with UNC119 (By similarity). The GTP-bound form interacts with
CC       GOLGA1 and GOLGA4. {ECO:0000250, ECO:0000269|PubMed:12972563,
CC       ECO:0000269|PubMed:14718928}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:12972563}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12972563}; Cytoplasmic side
CC       {ECO:0000269|PubMed:12972563}. Membrane {ECO:0000250|UniProtKB:P40616};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P40616}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; X76920; CAA54245.1; -; mRNA.
DR   EMBL; U12402; AAA20668.1; -; mRNA.
DR   EMBL; BC061553; AAH61553.1; -; mRNA.
DR   PIR; A54022; A54022.
DR   RefSeq; NP_071780.1; NM_022385.3.
DR   PDB; 1R4A; X-ray; 2.30 A; A/B/C/D=16-180.
DR   PDBsum; 1R4A; -.
DR   AlphaFoldDB; P61212; -.
DR   SMR; P61212; -.
DR   IntAct; P61212; 2.
DR   STRING; 10116.ENSRNOP00000007623; -.
DR   iPTMnet; P61212; -.
DR   PhosphoSitePlus; P61212; -.
DR   jPOST; P61212; -.
DR   PaxDb; P61212; -.
DR   PeptideAtlas; P61212; -.
DR   PRIDE; P61212; -.
DR   GeneID; 64187; -.
DR   KEGG; rno:64187; -.
DR   UCSC; RGD:621326; rat.
DR   CTD; 400; -.
DR   RGD; 621326; Arl1.
DR   VEuPathDB; HostDB:ENSRNOG00000005763; -.
DR   eggNOG; KOG0072; Eukaryota.
DR   HOGENOM; CLU_040729_9_4_1; -.
DR   InParanoid; P61212; -.
DR   OMA; QEGMDWL; -.
DR   OrthoDB; 1271528at2759; -.
DR   PhylomeDB; P61212; -.
DR   Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   EvolutionaryTrace; P61212; -.
DR   PRO; PR:P61212; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000005763; Expressed in stomach and 20 other tissues.
DR   Genevisible; P61212; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR   GO; GO:0008047; F:enzyme activator activity; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0031584; P:activation of phospholipase D activity; ISS:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IMP:RGD.
DR   GO; GO:0048193; P:Golgi vesicle transport; IMP:RGD.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   GO; GO:0009404; P:toxin metabolic process; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; PTHR11711; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Golgi apparatus; GTP-binding; Lipoprotein; Magnesium;
KW   Membrane; Metal-binding; Myristate; Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P40616"
FT   CHAIN           2..181
FT                   /note="ADP-ribosylation factor-like protein 1"
FT                   /id="PRO_0000207452"
FT   BINDING         24..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         31
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:14718928"
FT   BINDING         45..48
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:14718928"
FT   BINDING         48
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:14718928"
FT   BINDING         67..71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         160..161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P40616"
FT   MUTAGEN         2
FT                   /note="G->A: Abolishes association with the Golgi
FT                   apparatus."
FT                   /evidence="ECO:0000269|PubMed:11792819"
FT   MUTAGEN         31
FT                   /note="T->N: Accumulation of GDP-bound form."
FT                   /evidence="ECO:0000269|PubMed:11792819"
FT   MUTAGEN         71
FT                   /note="Q->L: Accumulation of GTP-bound form."
FT                   /evidence="ECO:0000269|PubMed:11792819"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   HELIX           30..36
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   STRAND          49..60
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   STRAND          87..95
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   HELIX           100..112
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   HELIX           136..143
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:1R4A"
FT   HELIX           166..179
FT                   /evidence="ECO:0007829|PDB:1R4A"
SQ   SEQUENCE   181 AA;  20412 MW;  3DFC4CC8ED632FEB CRC64;
     MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN
     LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI
     LVVFANKQDM EQAMTPSEMA NALGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR
     Q
 
 
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