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AR13B_DANRE
ID   AR13B_DANRE             Reviewed;         407 AA.
AC   Q8JHI3; Q561Z5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ADP-ribosylation factor-like protein 13B;
DE   AltName: Full=ADP-ribosylation factor-like protein 2-like 1;
DE            Short=ARL2-like protein 1;
DE   AltName: Full=Protein scorpion;
GN   Name=arl13b; Synonyms=arl2l1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND FUNCTION.
RC   TISSUE=Embryo;
RX   PubMed=12006978; DOI=10.1038/ng896;
RA   Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
RA   Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
RA   Hopkins N.;
RT   "Insertional mutagenesis in zebrafish rapidly identifies genes essential
RT   for early vertebrate development.";
RL   Nat. Genet. 31:135-140(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-275.
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15269167; DOI=10.1242/dev.01240;
RA   Sun Z., Amsterdam A., Pazour G.J., Cole D.G., Miller M.S., Hopkins N.;
RT   "A genetic screen in zebrafish identifies cilia genes as a principal cause
RT   of cystic kidney.";
RL   Development 131:4085-4093(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND MUTAGENESIS OF GLY-28 AND THR-35.
RX   PubMed=19906870; DOI=10.1242/dev.036350;
RA   Duldulao N.A., Lee S., Sun Z.;
RT   "Cilia localization is essential for in vivo functions of the Joubert
RT   syndrome protein Arl13b/Scorpion.";
RL   Development 136:4033-4042(2009).
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. Binds GTP but is not able
CC       to hydrolyze it; the GTPase activity remains unclear. Required to
CC       pattern the neural tube. Involved in cerebral cortex development:
CC       required for the initial formation of a polarized radial glial
CC       scaffold, the first step in the construction of the cerebral cortex, by
CC       regulating ciliary signaling. Regulates the migration and placement of
CC       postmitotic interneurons in the developing cerebral cortex Required
CC       during embryogenesis for cilia formation in multiple organs such as the
CC       pronephric duct. {ECO:0000269|PubMed:12006978,
CC       ECO:0000269|PubMed:15269167, ECO:0000269|PubMed:19906870}.
CC   -!- SUBUNIT: Interacts with EXOC2; regulates ARL13B localization to the
CC       cilium membrane. {ECO:0000250|UniProtKB:Q640N2}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC       {ECO:0000269|PubMed:19906870}; Lipid-anchor
CC       {ECO:0000269|PubMed:19906870}. Note=Associates to the cilium membrane
CC       via palmitoylation. Localizes to proximal ciliary membranes, to an
CC       inversin-like subciliary membrane compartment, excluding the transition
CC       zone.
CC   -!- TISSUE SPECIFICITY: Cilium-specific. {ECO:0000269|PubMed:19906870}.
CC   -!- DEVELOPMENTAL STAGE: Detected at the 4- to 32-cell stage, suggesting it
CC       is expressed maternally. {ECO:0000269|PubMed:19906870}.
CC   -!- DISRUPTION PHENOTYPE: Embryos have a ventrally curved tail, ciliary
CC       defects and cystic kidneys. {ECO:0000269|PubMed:15269167}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH92689.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF506213; AAM34657.1; -; mRNA.
DR   EMBL; BC092689; AAH92689.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_775379.1; NM_173272.1.
DR   AlphaFoldDB; Q8JHI3; -.
DR   SMR; Q8JHI3; -.
DR   STRING; 7955.ENSDARP00000092960; -.
DR   PaxDb; Q8JHI3; -.
DR   Ensembl; ENSDART00000102184; ENSDARP00000092960; ENSDARG00000012763.
DR   GeneID; 286784; -.
DR   KEGG; dre:286784; -.
DR   CTD; 200894; -.
DR   ZFIN; ZDB-GENE-021217-3; arl13b.
DR   eggNOG; KOG0074; Eukaryota.
DR   eggNOG; KOG0076; Eukaryota.
DR   GeneTree; ENSGT00940000156365; -.
DR   HOGENOM; CLU_040729_3_0_1; -.
DR   InParanoid; Q8JHI3; -.
DR   OrthoDB; 732329at2759; -.
DR   PhylomeDB; Q8JHI3; -.
DR   TreeFam; TF105476; -.
DR   Reactome; R-DRE-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
DR   Reactome; R-DRE-9013406; RHOQ GTPase cycle.
DR   Reactome; R-DRE-9013409; RHOJ GTPase cycle.
DR   Reactome; R-DRE-9646399; Aggrephagy.
DR   PRO; PR:Q8JHI3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 1.
DR   Bgee; ENSDARG00000012763; Expressed in testis and 28 other tissues.
DR   ExpressionAtlas; Q8JHI3; baseline.
DR   GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:ZFIN.
DR   GO; GO:0031514; C:motile cilium; IBA:GO_Central.
DR   GO; GO:0097730; C:non-motile cilium; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR   GO; GO:0021943; P:formation of radial glial scaffolds; ISS:UniProtKB.
DR   GO; GO:0021830; P:interneuron migration from the subpallium to the cortex; ISS:UniProtKB.
DR   GO; GO:0021532; P:neural tube patterning; ISS:UniProtKB.
DR   GO; GO:1905515; P:non-motile cilium assembly; ISS:UniProtKB.
DR   GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:ZFIN.
DR   GO; GO:0097500; P:receptor localization to non-motile cilium; IBA:GO_Central.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
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   Cell membrane; Cell projection; Cilium; Coiled coil; Developmental protein;
KW   GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Palmitate;
KW   Reference proteome.
FT   CHAIN           1..407
FT                   /note="ADP-ribosylation factor-like protein 13B"
FT                   /id="PRO_0000251139"
FT   REGION          202..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          195..313
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        202..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..312
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         28..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..75
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           8
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           9
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         28
FT                   /note="G->V: Abolishes ability to rescue a arl13b mutant
FT                   when transfected, without affecting localization to
FT                   cilium."
FT                   /evidence="ECO:0000269|PubMed:19906870"
FT   MUTAGEN         35
FT                   /note="T->N: Abolishes ability to rescue a arl13b mutant
FT                   when transfected, without affecting localization to
FT                   cilium."
FT                   /evidence="ECO:0000269|PubMed:19906870"
FT   CONFLICT        43
FT                   /note="G -> E (in Ref. 2; AAH92689)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  46566 MW;  DE491E88F57FAEC9 CRC64;
     MFNLMANCCN WLKRWREPAR KVTLVMVGLD NAGKTATVRG IQGESPLDVA PTVGFSKVDL
     KQGKFEVTIF DLGGGKRIRG IWKNYYSESY GVVFVVDSSD VQRIQETRDT MAEVLRHPRI
     AGKPVLVLAN KQDQDGAMAE ADIIETLSLE KLVNENKCLC QIEPCSAVLG YGKKVDKSIK
     NGLNWLLNNI AKDYEAISER VQKDTAEQKA QEEQDKKERA ERVRRIREER DRQEREEAER
     EGRTLKEEEL DDVNMFNPFQ PINNVLTENQ DRLNREKEMQ RQRENGQQGS VQEQIALQDE
     EEEEEDEESE RQTPESTESG AVDQTKKKTR KLRLKRKHRV DPLRMEEAAP KSPTPPPLPV
     GWATPKVSRL PKLEPLGDTR HSDFYGKPLP PVAIRQRPNS DTHDVIS
 
 
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