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AR13B_HUMAN
ID   AR13B_HUMAN             Reviewed;         428 AA.
AC   Q3SXY8; D3DN29; G3V1S8; Q504W8; Q8TCL5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 141.
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;
GN   Name=ARL13B; Synonyms=ARL2L1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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   [5]
RP   IDENTIFICATION.
RX   PubMed=15314642; DOI=10.1038/ng1414;
RA   Fan Y., Esmail M.A., Ansley S.J., Blacque O.E., Boroevich K., Ross A.J.,
RA   Moore S.J., Badano J.L., May-Simera H., Compton D.S., Green J.S.,
RA   Lewis R.A., van Haelst M.M., Parfrey P.S., Baillie D.L., Beales P.L.,
RA   Katsanis N., Davidson W.S., Leroux M.R.;
RT   "Mutations in a member of the Ras superfamily of small GTP-binding proteins
RT   causes Bardet-Biedl syndrome.";
RL   Nat. Genet. 36:989-993(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, GTP-BINDING, AND MUTAGENESIS OF THR-35 AND ASN-130.
RX   PubMed=18554500; DOI=10.1016/j.bbrc.2008.06.001;
RA   Hori Y., Kobayashi T., Kikko Y., Kontani K., Katada T.;
RT   "Domain architecture of the atypical Arf-family GTPase Arl13b involved in
RT   cilia formation.";
RL   Biochem. Biophys. Res. Commun. 373:119-124(2008).
RN   [7]
RP   INTERACTION WITH PIFO.
RX   PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA   Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA   Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT   "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL   Dev. Cell 19:66-77(2010).
RN   [8]
RP   SUMOYLATION AT LYS-329, AND MUTAGENESIS OF LYS-231; LYS-270; LYS-275;
RP   LYS-276; LYS-279 AND LYS-329.
RX   PubMed=23128241; DOI=10.1083/jcb.201203150;
RA   Li Y., Zhang Q., Wei Q., Zhang Y., Ling K., Hu J.;
RT   "SUMOylation of the small GTPase ARL-13 promotes ciliary targeting of
RT   sensory receptors.";
RL   J. Cell Biol. 199:589-598(2012).
RN   [9]
RP   INTERACTION WITH IFT46 AND IFT74.
RX   PubMed=24339792; DOI=10.1371/journal.pgen.1003977;
RA   Cevik S., Sanders A.A., Van Wijk E., Boldt K., Clarke L., van Reeuwijk J.,
RA   Hori Y., Horn N., Hetterschijt L., Wdowicz A., Mullins A., Kida K.,
RA   Kaplan O.I., van Beersum S.E., Man Wu K., Letteboer S.J., Mans D.A.,
RA   Katada T., Kontani K., Ueffing M., Roepman R., Kremer H., Blacque O.E.;
RT   "Active transport and diffusion barriers restrict Joubert syndrome-
RT   associated ARL13B/ARL-13 to an inv-like ciliary membrane subdomain.";
RL   PLoS Genet. 9:E1003977-E1003977(2013).
RN   [10]
RP   FUNCTION.
RX   PubMed=23150559; DOI=10.1073/pnas.1210916109;
RA   Humbert M.C., Weihbrecht K., Searby C.C., Li Y., Pope R.M., Sheffield V.C.,
RA   Seo S.;
RT   "ARL13B, PDE6D, and CEP164 form a functional network for INPP5E ciliary
RT   targeting.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:19691-19696(2012).
RN   [11]
RP   POSSIBLE FUNCTION.
RX   PubMed=23223633; DOI=10.1073/pnas.1218272110;
RA   Barral D.C., Garg S., Casalou C., Watts G.F., Sandoval J.L., Ramalho J.S.,
RA   Hsu V.W., Brenner M.B.;
RT   "Arl13b regulates endocytic recycling traffic.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:21354-21359(2012).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24120134; DOI=10.1016/j.cell.2013.08.060;
RA   Paridaen J.T., Wilsch-Brauninger M., Huttner W.B.;
RT   "Asymmetric inheritance of centrosome-associated primary cilium membrane
RT   directs ciliogenesis after cell division.";
RL   Cell 155:333-344(2013).
RN   [13]
RP   INVOLVEMENT IN JBTS8, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT
RP   JBTS8 CYS-86, AND CHARACTERIZATION OF VARIANT JBTS8 CYS-86.
RX   PubMed=25138100; DOI=10.1038/ejhg.2014.156;
RA   Thomas S., Cantagrel V., Mariani L., Serre V., Lee J.E., Elkhartoufi N.,
RA   de Lonlay P., Desguerre I., Munnich A., Boddaert N., Lyonnet S.,
RA   Vekemans M., Lisgo S.N., Caspary T., Gleeson J., Attie-Bitach T.;
RT   "Identification of a novel ARL13B variant in a Joubert syndrome-affected
RT   patient with retinal impairment and obesity.";
RL   Eur. J. Hum. Genet. 23:621-627(2015).
RN   [14]
RP   VARIANTS JBTS8 GLN-79 AND CYS-200, AND CHARACTERIZATION OF VARIANT JBTS8
RP   GLN-79.
RX   PubMed=18674751; DOI=10.1016/j.ajhg.2008.06.023;
RG   The international Joubert syndrome related disorders (JSRD) study group;
RA   Cantagrel V., Silhavy J.L., Bielas S.L., Swistun D., Marsh S.E.,
RA   Bertrand J.Y., Audollent S., Attie-Bitach T., Holden K.R., Dobyns W.B.,
RA   Traver D., Al-Gazali L., Ali B.R., Lindner T.H., Caspary T., Otto E.A.,
RA   Hildebrandt F., Glass I.A., Logan C.V., Johnson C.A., Bennett C.,
RA   Brancati F., Valente E.M., Woods C.G., Gleeson J.G.;
RT   "Mutations in the cilia gene ARL13B lead to the classical form of Joubert
RT   syndrome.";
RL   Am. J. Hum. Genet. 83:170-179(2008).
RN   [15]
RP   VARIANT LEU-390.
RX   PubMed=21068128; DOI=10.1136/jmg.2010.082552;
RA   Otto E.A., Ramaswami G., Janssen S., Chaki M., Allen S.J., Zhou W.,
RA   Airik R., Hurd T.W., Ghosh A.K., Wolf M.T., Hoppe B., Neuhaus T.J.,
RA   Bockenhauer D., Milford D.V., Soliman N.A., Antignac C., Saunier S.,
RA   Johnson C.A., Hildebrandt F.;
RT   "Mutation analysis of 18 nephronophthisis associated ciliopathy disease
RT   genes using a DNA pooling and next generation sequencing strategy.";
RL   J. Med. Genet. 48:105-116(2011).
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. May
CC       regulate endocytic recycling traffic; however, additional evidence is
CC       required to confirm these data. {ECO:0000269|PubMed:23150559}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with PIFO. Interacts with
CC       IFT complex B components IFT46 and IFT74 (By similarity)
CC       (PubMed:20643351, PubMed:24339792). Interacts with EXOC2; regulates
CC       ARL13B localization to the cilium membrane.
CC       {ECO:0000250|UniProtKB:Q640N2, ECO:0000269|PubMed:20643351,
CC       ECO:0000269|PubMed:24339792}.
CC   -!- INTERACTION:
CC       Q3SXY8; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-11343438, EBI-2876502;
CC       Q3SXY8; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-11343438, EBI-11957045;
CC       Q3SXY8; Q92685: ALG3; NbExp=3; IntAct=EBI-11343438, EBI-2848814;
CC       Q3SXY8; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-11343438, EBI-12109402;
CC       Q3SXY8; Q16853: AOC3; NbExp=3; IntAct=EBI-11343438, EBI-3921628;
CC       Q3SXY8; Q96PS8: AQP10; NbExp=3; IntAct=EBI-11343438, EBI-12820279;
CC       Q3SXY8; Q8NHY0: B4GALNT2; NbExp=3; IntAct=EBI-11343438, EBI-1042940;
CC       Q3SXY8; O95393: BMP10; NbExp=3; IntAct=EBI-11343438, EBI-3922513;
CC       Q3SXY8; Q12983: BNIP3; NbExp=3; IntAct=EBI-11343438, EBI-749464;
CC       Q3SXY8; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-11343438, EBI-12244618;
CC       Q3SXY8; O14523: C2CD2L; NbExp=3; IntAct=EBI-11343438, EBI-12822627;
CC       Q3SXY8; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-11343438, EBI-12003442;
CC       Q3SXY8; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-11343438, EBI-9083477;
CC       Q3SXY8; P13236: CCL4; NbExp=3; IntAct=EBI-11343438, EBI-2873970;
CC       Q3SXY8; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-11343438, EBI-10271156;
CC       Q3SXY8; P48509: CD151; NbExp=3; IntAct=EBI-11343438, EBI-10210332;
CC       Q3SXY8; Q8IX05: CD302; NbExp=3; IntAct=EBI-11343438, EBI-14259393;
CC       Q3SXY8; P19397: CD53; NbExp=3; IntAct=EBI-11343438, EBI-6657396;
CC       Q3SXY8; O14735: CDIPT; NbExp=3; IntAct=EBI-11343438, EBI-358858;
CC       Q3SXY8; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-11343438, EBI-11579371;
CC       Q3SXY8; O14493: CLDN4; NbExp=3; IntAct=EBI-11343438, EBI-9316372;
CC       Q3SXY8; P56748: CLDN8; NbExp=3; IntAct=EBI-11343438, EBI-10215641;
CC       Q3SXY8; Q6UXB4: CLEC4G; NbExp=3; IntAct=EBI-11343438, EBI-2114729;
CC       Q3SXY8; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-11343438, EBI-11989440;
CC       Q3SXY8; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-11343438, EBI-6165897;
CC       Q3SXY8; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-11343438, EBI-7247651;
CC       Q3SXY8; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-11343438, EBI-2807956;
CC       Q3SXY8; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-11343438, EBI-10241815;
CC       Q3SXY8; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-11343438, EBI-10267100;
CC       Q3SXY8; O14569: CYB561D2; NbExp=3; IntAct=EBI-11343438, EBI-717654;
CC       Q3SXY8; Q15125: EBP; NbExp=3; IntAct=EBI-11343438, EBI-3915253;
CC       Q3SXY8; P54849: EMP1; NbExp=3; IntAct=EBI-11343438, EBI-4319440;
CC       Q3SXY8; O75355-2: ENTPD3; NbExp=3; IntAct=EBI-11343438, EBI-12279764;
CC       Q3SXY8; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-11343438, EBI-12142299;
CC       Q3SXY8; P37268: FDFT1; NbExp=3; IntAct=EBI-11343438, EBI-714550;
CC       Q3SXY8; Q14318: FKBP8; NbExp=3; IntAct=EBI-11343438, EBI-724839;
CC       Q3SXY8; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-11343438, EBI-714482;
CC       Q3SXY8; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-11343438, EBI-713304;
CC       Q3SXY8; Q05329: GAD2; NbExp=3; IntAct=EBI-11343438, EBI-9304251;
CC       Q3SXY8; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-11343438, EBI-11991950;
CC       Q3SXY8; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-11343438, EBI-6166686;
CC       Q3SXY8; P29033: GJB2; NbExp=3; IntAct=EBI-11343438, EBI-3905204;
CC       Q3SXY8; O14653: GOSR2; NbExp=3; IntAct=EBI-11343438, EBI-4401517;
CC       Q3SXY8; O60883: GPR37L1; NbExp=3; IntAct=EBI-11343438, EBI-2927498;
CC       Q3SXY8; P09601: HMOX1; NbExp=3; IntAct=EBI-11343438, EBI-2806151;
CC       Q3SXY8; P30519: HMOX2; NbExp=3; IntAct=EBI-11343438, EBI-712096;
CC       Q3SXY8; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-11343438, EBI-748420;
CC       Q3SXY8; O60725: ICMT; NbExp=3; IntAct=EBI-11343438, EBI-11721771;
CC       Q3SXY8; P11215: ITGAM; NbExp=3; IntAct=EBI-11343438, EBI-2568251;
CC       Q3SXY8; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-11343438, EBI-10266796;
CC       Q3SXY8; P63252: KCNJ2; NbExp=4; IntAct=EBI-11343438, EBI-703457;
CC       Q3SXY8; Q96E93: KLRG1; NbExp=3; IntAct=EBI-11343438, EBI-750770;
CC       Q3SXY8; O95214: LEPROTL1; NbExp=3; IntAct=EBI-11343438, EBI-750776;
CC       Q3SXY8; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-11343438, EBI-12033434;
CC       Q3SXY8; Q969L2: MAL2; NbExp=3; IntAct=EBI-11343438, EBI-944295;
CC       Q3SXY8; Q13021: MALL; NbExp=3; IntAct=EBI-11343438, EBI-750078;
CC       Q3SXY8; Q15546: MMD; NbExp=3; IntAct=EBI-11343438, EBI-17873222;
CC       Q3SXY8; O75425: MOSPD3; NbExp=3; IntAct=EBI-11343438, EBI-12179105;
CC       Q3SXY8; Q96DR8: MUCL1; NbExp=3; IntAct=EBI-11343438, EBI-9056153;
CC       Q3SXY8; A6NDP7: MYADML2; NbExp=3; IntAct=EBI-11343438, EBI-17641390;
CC       Q3SXY8; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-11343438, EBI-2863634;
CC       Q3SXY8; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-11343438, EBI-10317425;
CC       Q3SXY8; Q16617: NKG7; NbExp=3; IntAct=EBI-11343438, EBI-3919611;
CC       Q3SXY8; Q8IXM6: NRM; NbExp=3; IntAct=EBI-11343438, EBI-10262547;
CC       Q3SXY8; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-11343438, EBI-1054848;
CC       Q3SXY8; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-11343438, EBI-721750;
CC       Q3SXY8; P09466: PAEP; NbExp=3; IntAct=EBI-11343438, EBI-465167;
CC       Q3SXY8; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-11343438, EBI-716063;
CC       Q3SXY8; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-11343438, EBI-12092917;
CC       Q3SXY8; P26678: PLN; NbExp=3; IntAct=EBI-11343438, EBI-692836;
CC       Q3SXY8; P60201-2: PLP1; NbExp=3; IntAct=EBI-11343438, EBI-12188331;
CC       Q3SXY8; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-11343438, EBI-10485931;
CC       Q3SXY8; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-11343438, EBI-12955265;
CC       Q3SXY8; Q01453: PMP22; NbExp=3; IntAct=EBI-11343438, EBI-2845982;
CC       Q3SXY8; Q59EV6: PPGB; NbExp=3; IntAct=EBI-11343438, EBI-14210385;
CC       Q3SXY8; A5D903: PRB1; NbExp=3; IntAct=EBI-11343438, EBI-10173935;
CC       Q3SXY8; P43378: PTPN9; NbExp=3; IntAct=EBI-11343438, EBI-742898;
CC       Q3SXY8; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-11343438, EBI-10244780;
CC       Q3SXY8; P29034: S100A2; NbExp=3; IntAct=EBI-11343438, EBI-752230;
CC       Q3SXY8; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-11343438, EBI-3917235;
CC       Q3SXY8; Q9NTN9-2: SEMA4G; NbExp=3; IntAct=EBI-11343438, EBI-12913124;
CC       Q3SXY8; Q8WWT9: SLC13A3; NbExp=3; IntAct=EBI-11343438, EBI-12938720;
CC       Q3SXY8; P22732: SLC2A5; NbExp=3; IntAct=EBI-11343438, EBI-2825135;
CC       Q3SXY8; P78382: SLC35A1; NbExp=3; IntAct=EBI-11343438, EBI-12870360;
CC       Q3SXY8; P78383: SLC35B1; NbExp=3; IntAct=EBI-11343438, EBI-12147661;
CC       Q3SXY8; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-11343438, EBI-10314552;
CC       Q3SXY8; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-11343438, EBI-12898013;
CC       Q3SXY8; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-11343438, EBI-10226799;
CC       Q3SXY8; P16150: SPN; NbExp=3; IntAct=EBI-11343438, EBI-10049055;
CC       Q3SXY8; P0DN84: STRIT1; NbExp=3; IntAct=EBI-11343438, EBI-12200293;
CC       Q3SXY8; Q16623: STX1A; NbExp=3; IntAct=EBI-11343438, EBI-712466;
CC       Q3SXY8; O15400: STX7; NbExp=3; IntAct=EBI-11343438, EBI-3221827;
CC       Q3SXY8; Q9NZ01: TECR; NbExp=3; IntAct=EBI-11343438, EBI-2877718;
CC       Q3SXY8; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-11343438, EBI-10329860;
CC       Q3SXY8; P02786: TFRC; NbExp=3; IntAct=EBI-11343438, EBI-355727;
CC       Q3SXY8; Q9UPZ6: THSD7A; NbExp=3; IntAct=EBI-11343438, EBI-310962;
CC       Q3SXY8; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-11343438, EBI-17192156;
CC       Q3SXY8; Q9BZW4: TM6SF2; NbExp=3; IntAct=EBI-11343438, EBI-13082040;
CC       Q3SXY8; P17152: TMEM11; NbExp=3; IntAct=EBI-11343438, EBI-723946;
CC       Q3SXY8; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-11343438, EBI-12155101;
CC       Q3SXY8; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-11343438, EBI-10694905;
CC       Q3SXY8; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-11343438, EBI-2339195;
CC       Q3SXY8; Q14656: TMEM187; NbExp=3; IntAct=EBI-11343438, EBI-13046724;
CC       Q3SXY8; Q8WZ59: TMEM190; NbExp=3; IntAct=EBI-11343438, EBI-10278423;
CC       Q3SXY8; A2RU14: TMEM218; NbExp=3; IntAct=EBI-11343438, EBI-10173151;
CC       Q3SXY8; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-11343438, EBI-12195227;
CC       Q3SXY8; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-11343438, EBI-11956809;
CC       Q3SXY8; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-11343438, EBI-721293;
CC       Q3SXY8; Q969K7: TMEM54; NbExp=3; IntAct=EBI-11343438, EBI-3922833;
CC       Q3SXY8; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-11343438, EBI-6656213;
CC       Q3SXY8; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-11343438, EBI-8649725;
CC       Q3SXY8; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-11343438, EBI-2548832;
CC       Q3SXY8; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-11343438, EBI-12111910;
CC       Q3SXY8; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-11343438, EBI-2820477;
CC       Q3SXY8; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-11343438, EBI-717441;
CC       Q3SXY8; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-11343438, EBI-12003398;
CC       Q3SXY8; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-11343438, EBI-12195249;
CC       Q3SXY8; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-11343438, EBI-11988865;
CC       Q3SXY8; P23763-3: VAMP1; NbExp=3; IntAct=EBI-11343438, EBI-12097582;
CC       Q3SXY8; P63027: VAMP2; NbExp=3; IntAct=EBI-11343438, EBI-520113;
CC       Q3SXY8; Q15836: VAMP3; NbExp=3; IntAct=EBI-11343438, EBI-722343;
CC       Q3SXY8; O75379: VAMP4; NbExp=3; IntAct=EBI-11343438, EBI-744953;
CC       Q3SXY8; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-11343438, EBI-12190699;
CC       Q3SXY8; Q14508: WFDC2; NbExp=3; IntAct=EBI-11343438, EBI-723529;
CC       Q3SXY8; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-11343438, EBI-751210;
CC       Q3SXY8; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-11343438, EBI-12837904;
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC       {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}; Lipid-
CC       anchor {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}. Cell
CC       projection, cilium {ECO:0000269|PubMed:25138100}. Note=Associates to
CC       the cilium membrane via palmitoylation. Localizes to proximal ciliary
CC       membranes, to an inversin-like subciliary membrane compartment,
CC       excluding the transition zone.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3SXY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3SXY8-2; Sequence=VSP_020733;
CC       Name=3;
CC         IsoId=Q3SXY8-3; Sequence=VSP_045421;
CC   -!- TISSUE SPECIFICITY: Expressed in the developing brain.
CC       {ECO:0000269|PubMed:25138100}.
CC   -!- PTM: Sumoylation is required for PKD2 entry into cilium.
CC       {ECO:0000269|PubMed:23128241}.
CC   -!- DISEASE: Joubert syndrome 8 (JBTS8) [MIM:612291]: A disorder presenting
CC       with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal
CC       breathing abnormalities and psychomotor delay. Neuroradiologically, it
CC       is characterized by cerebellar vermian hypoplasia/aplasia, thickened
CC       and reoriented superior cerebellar peduncles, and an abnormally large
CC       interpeduncular fossa, giving the appearance of a molar tooth on
CC       transaxial slices (molar tooth sign). Additional variable features
CC       include retinal dystrophy and renal disease.
CC       {ECO:0000269|PubMed:18674751, ECO:0000269|PubMed:25138100}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: Used as a ciliary marker because of its specific
CC       localization to microtubule doublets of the ciliary axoneme.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was initially thought to form a homodimer (PubMed:18554500).
CC       However, 3D structure of C.reinhardtii ortholog showed that it is
CC       probably not the case. {ECO:0000305|PubMed:18554500}.
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DR   EMBL; AL713789; CAD28544.2; -; mRNA.
DR   EMBL; AC117474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79897.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79901.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79898.1; -; Genomic_DNA.
DR   EMBL; BC094725; AAH94725.1; -; mRNA.
DR   EMBL; BC104035; AAI04036.1; -; mRNA.
DR   EMBL; BC104036; AAI04037.1; -; mRNA.
DR   CCDS; CCDS2924.1; -. [Q3SXY8-2]
DR   CCDS; CCDS2925.1; -. [Q3SXY8-1]
DR   CCDS; CCDS54615.1; -. [Q3SXY8-3]
DR   RefSeq; NP_001167621.1; NM_001174150.1. [Q3SXY8-1]
DR   RefSeq; NP_001167622.1; NM_001174151.1. [Q3SXY8-3]
DR   RefSeq; NP_659433.2; NM_144996.3. [Q3SXY8-2]
DR   RefSeq; NP_878899.1; NM_182896.2. [Q3SXY8-1]
DR   RefSeq; XP_016861342.1; XM_017005853.1. [Q3SXY8-3]
DR   AlphaFoldDB; Q3SXY8; -.
DR   SMR; Q3SXY8; -.
DR   BioGRID; 128353; 217.
DR   IntAct; Q3SXY8; 147.
DR   MINT; Q3SXY8; -.
DR   STRING; 9606.ENSP00000377769; -.
DR   iPTMnet; Q3SXY8; -.
DR   PhosphoSitePlus; Q3SXY8; -.
DR   SwissPalm; Q3SXY8; -.
DR   BioMuta; ARL13B; -.
DR   DMDM; 115503786; -.
DR   EPD; Q3SXY8; -.
DR   jPOST; Q3SXY8; -.
DR   MassIVE; Q3SXY8; -.
DR   MaxQB; Q3SXY8; -.
DR   PaxDb; Q3SXY8; -.
DR   PeptideAtlas; Q3SXY8; -.
DR   PRIDE; Q3SXY8; -.
DR   ProteomicsDB; 32429; -.
DR   ProteomicsDB; 61823; -. [Q3SXY8-1]
DR   ProteomicsDB; 61824; -. [Q3SXY8-2]
DR   Antibodypedia; 32073; 133 antibodies from 28 providers.
DR   DNASU; 200894; -.
DR   Ensembl; ENST00000303097.11; ENSP00000306225.7; ENSG00000169379.17. [Q3SXY8-2]
DR   Ensembl; ENST00000394222.8; ENSP00000377769.3; ENSG00000169379.17. [Q3SXY8-1]
DR   Ensembl; ENST00000471138.5; ENSP00000420780.1; ENSG00000169379.17. [Q3SXY8-1]
DR   Ensembl; ENST00000535334.5; ENSP00000445145.1; ENSG00000169379.17. [Q3SXY8-3]
DR   GeneID; 200894; -.
DR   KEGG; hsa:200894; -.
DR   MANE-Select; ENST00000394222.8; ENSP00000377769.3; NM_001174150.2; NP_001167621.1.
DR   UCSC; uc003drc.4; human. [Q3SXY8-1]
DR   CTD; 200894; -.
DR   DisGeNET; 200894; -.
DR   GeneCards; ARL13B; -.
DR   GeneReviews; ARL13B; -.
DR   HGNC; HGNC:25419; ARL13B.
DR   HPA; ENSG00000169379; Tissue enhanced (retina).
DR   MalaCards; ARL13B; -.
DR   MIM; 608922; gene.
DR   MIM; 612291; phenotype.
DR   neXtProt; NX_Q3SXY8; -.
DR   OpenTargets; ENSG00000169379; -.
DR   Orphanet; 475; Joubert syndrome.
DR   PharmGKB; PA134975272; -.
DR   VEuPathDB; HostDB:ENSG00000169379; -.
DR   eggNOG; KOG0074; Eukaryota.
DR   eggNOG; KOG0076; Eukaryota.
DR   GeneTree; ENSGT00940000156365; -.
DR   HOGENOM; CLU_040729_3_0_1; -.
DR   InParanoid; Q3SXY8; -.
DR   OMA; RPNGDAQ; -.
DR   OrthoDB; 732329at2759; -.
DR   PhylomeDB; Q3SXY8; -.
DR   TreeFam; TF105476; -.
DR   PathwayCommons; Q3SXY8; -.
DR   Reactome; R-HSA-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
DR   Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR   Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR   Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR   Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR   Reactome; R-HSA-9646399; Aggrephagy.
DR   SignaLink; Q3SXY8; -.
DR   BioGRID-ORCS; 200894; 18 hits in 1078 CRISPR screens.
DR   ChiTaRS; ARL13B; human.
DR   GeneWiki; ARL13B; -.
DR   GenomeRNAi; 200894; -.
DR   Pharos; Q3SXY8; Tbio.
DR   PRO; PR:Q3SXY8; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q3SXY8; protein.
DR   Bgee; ENSG00000169379; Expressed in secondary oocyte and 166 other tissues.
DR   ExpressionAtlas; Q3SXY8; baseline and differential.
DR   Genevisible; Q3SXY8; HS.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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; ISS:UniProtKB.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0021943; P:formation of radial glial scaffolds; ISS:UniProtKB.
DR   GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR   GO; GO:0021830; P:interneuron migration from the subpallium to the cortex; ISS:UniProtKB.
DR   GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR   GO; GO:0021532; P:neural tube patterning; ISS:UniProtKB.
DR   GO; GO:1905515; P:non-motile cilium assembly; ISS:UniProtKB.
DR   GO; GO:0097500; P:receptor localization to non-motile cilium; IBA:GO_Central.
DR   GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
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   Alternative splicing; Cell membrane; Cell projection; Ciliopathy; Cilium;
KW   Coiled coil; Disease variant; GTP-binding; Isopeptide bond;
KW   Joubert syndrome; Lipoprotein; Membrane; Nucleotide-binding; Palmitate;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..428
FT                   /note="ADP-ribosylation factor-like protein 13B"
FT                   /id="PRO_0000251137"
FT   REGION          207..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          192..245
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        207..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..346
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..385
FT                   /note="Pro 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   CROSSLNK        329
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         1..103
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_045421"
FT   VAR_SEQ         21..127
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020733"
FT   VARIANT         79
FT                   /note="R -> Q (in JBTS8; reduces binding to GTP;
FT                   dbSNP:rs121912606)"
FT                   /evidence="ECO:0000269|PubMed:18674751"
FT                   /id="VAR_054371"
FT   VARIANT         86
FT                   /note="Y -> C (in JBTS8; the patient also manifests obesity
FT                   as a feature; decreased localization to cilium;
FT                   dbSNP:rs863225430)"
FT                   /evidence="ECO:0000269|PubMed:25138100"
FT                   /id="VAR_077496"
FT   VARIANT         200
FT                   /note="R -> C (in JBTS8; dbSNP:rs121912608)"
FT                   /evidence="ECO:0000269|PubMed:18674751"
FT                   /id="VAR_054372"
FT   VARIANT         348
FT                   /note="T -> S (in dbSNP:rs33944211)"
FT                   /id="VAR_048319"
FT   VARIANT         390
FT                   /note="R -> L (in a nephronophthisis (NPHP) patient)"
FT                   /evidence="ECO:0000269|PubMed:21068128"
FT                   /id="VAR_069190"
FT   MUTAGEN         35
FT                   /note="T->N: Does not affect localization to cilia."
FT                   /evidence="ECO:0000269|PubMed:18554500"
FT   MUTAGEN         130
FT                   /note="N->I: Does not affect localization to cilia."
FT                   /evidence="ECO:0000269|PubMed:18554500"
FT   MUTAGEN         231
FT                   /note="K->R: No effect. Abolishes sumoylation; when
FT                   associated with R-270; R-275; R-276; R-279 and R-329."
FT                   /evidence="ECO:0000269|PubMed:23128241"
FT   MUTAGEN         270
FT                   /note="K->R: No effect. Abolishes sumoylation; when
FT                   associated with R-231; R-275; R-276; R-279 and R-329."
FT                   /evidence="ECO:0000269|PubMed:23128241"
FT   MUTAGEN         275
FT                   /note="K->R: No effect. Abolishes sumoylation; when
FT                   associated with R-231; R-270; R-276; R-279 and R-329."
FT                   /evidence="ECO:0000269|PubMed:23128241"
FT   MUTAGEN         276
FT                   /note="K->R: No effect. Abolishes sumoylation; when
FT                   associated with R-231; R-270; R-275; R-279 and R-329."
FT                   /evidence="ECO:0000269|PubMed:23128241"
FT   MUTAGEN         279
FT                   /note="K->R: No effect. Abolishes sumoylation; when
FT                   associated with R-231; R-270; R-275; R-276 and R-329."
FT                   /evidence="ECO:0000269|PubMed:23128241"
FT   MUTAGEN         329
FT                   /note="K->R: Abolishes sumoylation. Abolishes sumoylation;
FT                   when associated with R-231; R-270; R-275; R-276 and R-279."
FT                   /evidence="ECO:0000269|PubMed:23128241"
FT   CONFLICT        275
FT                   /note="K -> KK (in Ref. 1; CAD28544)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   428 AA;  48643 MW;  002B38A38D1F7BDD CRC64;
     MFSLMASCCG WFKRWREPVR KVTLLMVGLD NAGKTATAKG IQGEYPEDVA PTVGFSKINL
     RQGKFEVTIF DLGGGIRIRG IWKNYYAESY GVIFVVDSSD EERMEETKEA MSEMLRHPRI
     SGKPILVLAN KQDKEGALGE ADVIECLSLE KLVNEHKCLC QIEPCSAISG YGKKIDKSIK
     KGLYWLLHVI ARDFDALNER IQKETTEQRA LEEQEKQERA ERVRKLREER KQNEQEQAEL
     DGTSGLAELD PEPTNPFQPI ASVIIENEGK LEREKKNQKM EKDSDGCHLK HKMEHEQIET
     QGQVNHNGQK NNEFGLVENY KEALTQQLKN EDETDRPSLE SANGKKKTKK LRMKRNHRVE
     PLNIDDCAPE SPTPPPPPPP VGWGTPKVTR LPKLEPLGET HHNDFYRKPL PPLAVPQRPN
     SDAHDVIS
 
 
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