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ARL13_CHLRE
ID   ARL13_CHLRE             Reviewed;         527 AA.
AC   A8INQ0;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=ADP-ribosylation factor-like protein 13B;
DE            Short=CrArl13B;
GN   Name=ARL13; ORFNames=CHLREDRAFT_195529;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 18-242 IN COMPLEX WITH GTP, AND
RP   SUBUNIT.
RX   PubMed=24168557; DOI=10.1042/bj20131097;
RA   Miertzschke M., Koerner C., Spoerner M., Wittinghofer A.;
RT   "Structural insights into the small G-protein Arl13B and implications for
RT   Joubert syndrome.";
RL   Biochem. J. 457:301-311(2014).
CC   -!- FUNCTION: Cilium-specific protein required to control the microtubule-
CC       based, ciliary axoneme structure. May act by maintaining the
CC       association between IFT subcomplexes A and B (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24168557}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}.
CC   -!- DOMAIN: Contains an incomplete active site due to the presence of a Gly
CC       residue in position 72 instead of a Gln, probably explaining the
CC       inability to hydrolyze GTP. {ECO:0000269|PubMed:24168557}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; DS496119; EDP05163.1; -; Genomic_DNA.
DR   RefSeq; XP_001691430.1; XM_001691378.1.
DR   PDB; 4M9Q; X-ray; 2.50 A; A/B/C=18-242.
DR   PDB; 5DI3; X-ray; 2.50 A; B=18-278.
DR   PDBsum; 4M9Q; -.
DR   PDBsum; 5DI3; -.
DR   AlphaFoldDB; A8INQ0; -.
DR   SMR; A8INQ0; -.
DR   STRING; 3055.EDP05163; -.
DR   PaxDb; A8INQ0; -.
DR   PRIDE; A8INQ0; -.
DR   EnsemblPlants; PNW82955; PNW82955; CHLRE_06g301050v5.
DR   GeneID; 5716967; -.
DR   Gramene; PNW82955; PNW82955; CHLRE_06g301050v5.
DR   KEGG; cre:CHLRE_06g301050v5; -.
DR   eggNOG; KOG0074; Eukaryota.
DR   HOGENOM; CLU_517166_0_0_1; -.
DR   InParanoid; A8INQ0; -.
DR   OrthoDB; 732329at2759; -.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
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; Cell membrane; Cell projection; Cilium; GTP-binding;
KW   Membrane; Nucleotide-binding.
FT   CHAIN           1..527
FT                   /note="ADP-ribosylation factor-like protein 13B"
FT                   /id="PRO_0000425900"
FT   REGION          200..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26..33
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:24168557"
FT   BINDING         69..73
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..131
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:24168557"
FT   STRAND          18..25
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           32..39
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           77..86
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   STRAND          88..95
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           102..114
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           138..144
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           172..205
FT                   /evidence="ECO:0007829|PDB:4M9Q"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:4M9Q"
SQ   SEQUENCE   527 AA;  54793 MW;  F73AB844C85833DD CRC64;
     MFGLLVNFYR FCRKKTERKI TIALLGLDNA GKTTLLNSIQ GEVDRDTTPT FGFNSTTLNE
     GKYKIEVFDL GGGKNIRGVW KKYLAEVHAI VYVVDAADPG RFEESKMTMA EVLENQFMRD
     KPICIFANKQ DLPTAAPAAE VVKGLGLATC RNSHNVFPCT AKMPAGQDVD HRLRDGLKWL
     VGTVDREFGR LDPRVQTEAE EVRQEEARKK KEREERLRKQ REERLRQQKE EEERAREVEK
     ENELHDGKAP SLLAAGGGVV GAAAAGVNGV MVDEQQELRP PGQHQEAPEA LGLHNGLALG
     LPHTIESPGK FPPPPRRPLE AHPASDLRLV APDQGVSSAS GGPGLGAMPS GSHGGGGVPP
     QPASLPHVRA ALPPLPPSAP QPSDAGVGSS GSASRHPGAH SSSAAAPPNV ASGAAAEDGP
     EPDAAGTAAG EAGSGSVFAP RPASAGGGGP GSRGSGSGMT PDARELGSGG VESGEGTPAR
     LRAGAQQASD GGHGNSKGSF SLVHTSNKVV PVAPDLRAGI PGAPNDA
 
 
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