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ARL8B_HUMAN
ID   ARL8B_HUMAN             Reviewed;         186 AA.
AC   Q9NVJ2; B4DI85;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=ADP-ribosylation factor-like protein 8B {ECO:0000305};
DE            EC=3.6.5.2 {ECO:0000269|PubMed:15331635, ECO:0000269|PubMed:16537643};
DE   AltName: Full=ADP-ribosylation factor-like protein 10C;
DE   AltName: Full=Novel small G protein indispensable for equal chromosome segregation 1;
GN   Name=ARL8B {ECO:0000312|HGNC:HGNC:25564}; Synonyms=ARL10C, GIE1;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   MUTAGENESIS OF THR-34; 49-MET--ARG-58; TRP-70; 74-GLY--TYR-85 AND ASN-130,
RP   SUBCELLULAR LOCATION, INTERACTION WITH TUBULIN, AND CATALYTIC ACTIVITY.
RC   TISSUE=Brain;
RX   PubMed=15331635; DOI=10.1242/jcs.01347;
RA   Okai T., Araki Y., Tada M., Tateno T., Kontani K., Katada T.;
RT   "Novel small GTPase subfamily capable of associating with tubulin is
RT   required for chromosome segregation.";
RL   J. Cell Sci. 117:4705-4715(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Hippocampus, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic carcinoma, and Testis;
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   [7]
RP   PROTEIN SEQUENCE OF 69-77; 147-155 AND 166-182, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-34 AND GLN-75.
RX   PubMed=16650381; DOI=10.1016/j.bbrc.2006.03.221;
RA   Bagshaw R.D., Callahan J.W., Mahuran D.J.;
RT   "The Arf-family protein, Arl8b, is involved in the spatial distribution of
RT   lysosomes.";
RL   Biochem. Biophys. Res. Commun. 344:1186-1191(2006).
RN   [9]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   ACETYLATION AT MET-1, MUTAGENESIS OF LEU-2; 5-ILE--PHE-12 AND GLN-75, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=16537643; DOI=10.1242/jcs.02958;
RA   Hofmann I., Munro S.;
RT   "An N-terminally acetylated Arf-like GTPase is localised to lysosomes and
RT   affects their motility.";
RL   J. Cell Sci. 119:1494-1503(2006).
RN   [10]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Placenta;
RX   PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA   Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA   Elsaesser H.-P., Mann M., Hasilik A.;
RT   "Integral and associated lysosomal membrane proteins.";
RL   Traffic 8:1676-1686(2007).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   FUNCTION, INTERACTION WITH PLEKHM2, AND SUBCELLULAR LOCATION.
RX   PubMed=22172677; DOI=10.1016/j.devcel.2011.10.007;
RA   Rosa-Ferreira C., Munro S.;
RT   "Arl8 and SKIP act together to link lysosomes to kinesin-1.";
RL   Dev. Cell 21:1171-1178(2011).
RN   [13]
RP   FUNCTION, INTERACTION WITH VPS41, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   THR-34 AND GLN-75.
RX   PubMed=21802320; DOI=10.1016/j.immuni.2011.06.009;
RA   Garg S., Sharma M., Ung C., Tuli A., Barral D.C., Hava D.L., Veerapen N.,
RA   Besra G.S., Hacohen N., Brenner M.B.;
RT   "Lysosomal trafficking, antigen presentation, and microbial killing are
RT   controlled by the Arf-like GTPase Arl8b.";
RL   Immunity 35:182-193(2011).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24088571; DOI=10.1091/mbc.e13-05-0259;
RA   Tuli A., Thiery J., James A.M., Michelet X., Sharma M., Garg S.,
RA   Sanborn K.B., Orange J.S., Lieberman J., Brenner M.B.;
RT   "Arf-like GTPase Arl8b regulates lytic granule polarization and natural
RT   killer cell-mediated cytotoxicity.";
RL   Mol. Biol. Cell 24:3721-3735(2013).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   FUNCTION, INTERACTION WITH BORCS5, AND SUBCELLULAR LOCATION.
RX   PubMed=25898167; DOI=10.1016/j.devcel.2015.02.011;
RA   Pu J., Schindler C., Jia R., Jarnik M., Backlund P., Bonifacino J.S.;
RT   "BORC, a multisubunit complex that regulates lysosome positioning.";
RL   Dev. Cell 33:176-188(2015).
RN   [19]
RP   FUNCTION, AND INTERACTION WITH VPS41.
RX   PubMed=25908847; DOI=10.1242/jcs.162651;
RA   Khatter D., Raina V.B., Dwivedi D., Sindhwani A., Bahl S., Sharma M.;
RT   "The small GTPase Arl8b regulates assembly of the mammalian HOPS complex on
RT   lysosomes.";
RL   J. Cell Sci. 128:1746-1761(2015).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [21]
RP   FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-141, AND MUTAGENESIS
RP   OF LYS-141.
RX   PubMed=27808481; DOI=10.1111/febs.13947;
RA   Deshar R., Moon S., Yoo W., Cho E.B., Yoon S.K., Yoon J.B.;
RT   "RNF167 targets Arl8B for degradation to regulate lysosome positioning and
RT   endocytic trafficking.";
RL   FEBS J. 283:4583-4599(2016).
RN   [22]
RP   FUNCTION, INTERACTION WITH PLEKHM1 AND PLEKHM2, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF THR-34 AND GLN-75.
RX   PubMed=28325809; DOI=10.1083/jcb.201607085;
RA   Marwaha R., Arya S.B., Jagga D., Kaur H., Tuli A., Sharma M.;
RT   "The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to
RT   lysosomes.";
RL   J. Cell Biol. 216:1051-1070(2017).
RN   [23]
RP   FUNCTION (MICROBIAL INFECTION), FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=29592961; DOI=10.4049/jimmunol.1700829;
RA   Michelet X., Tuli A., Gan H., Geadas C., Sharma M., Remold H.G.,
RA   Brenner M.B.;
RT   "Lysosome-Mediated Plasma Membrane Repair Is Dependent on the Small GTPase
RT   Arl8b and Determines Cell Death Type in Mycobacterium tuberculosis
RT   Infection.";
RL   J. Immunol. 200:3160-3169(2018).
RN   [24]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=33157038; DOI=10.1016/j.cell.2020.10.039;
RA   Ghosh S., Dellibovi-Ragheb T.A., Kerviel A., Pak E., Qiu Q., Fisher M.,
RA   Takvorian P.M., Bleck C., Hsu V.W., Fehr A.R., Perlman S., Achar S.R.,
RA   Straus M.R., Whittaker G.R., de Haan C.A.M., Kehrl J., Altan-Bonnet G.,
RA   Altan-Bonnet N.;
RT   "beta-Coronaviruses Use Lysosomes for Egress Instead of the Biosynthetic
RT   Secretory Pathway.";
RL   Cell 183:1520-1535(2020).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 18-184 IN COMPLEX WITH GDP.
RG   Structural genomics consortium (SGC);
RT   "GTP-like conformation of GDP-bound ARL10C GTPase.";
RL   Submitted (AUG-2005) to the PDB data bank.
CC   -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC       inactive GDP-bound states (PubMed:15331635, PubMed:16537643). In its
CC       active state, binds to a variety of effector proteins playing a key
CC       role in the regulation of lysosomal positioning which is important for
CC       nutrient sensing, natural killer cell-mediated cytotoxicity and antigen
CC       presentation. Along with its effectors, orchestrates lysosomal
CC       transport and fusion (PubMed:16650381, PubMed:16537643,
CC       PubMed:28325809, PubMed:25898167, PubMed:27808481). Localizes
CC       specifically to lysosomal membranes and mediates anterograde lysosomal
CC       motility by recruiting PLEKHM2, which in turn recruits the motor
CC       protein kinesin-1 on lysosomes. Required for lysosomal and cytolytic
CC       granule exocytosis (PubMed:22172677, PubMed:29592961, PubMed:24088571).
CC       Critical factor involved in NK cell-mediated cytotoxicity. Drives the
CC       polarization of cytolytic granules and microtubule-organizing centers
CC       (MTOCs) toward the immune synapse between effector NK lymphocytes and
CC       target cells (PubMed:24088571). In neurons, mediates the anterograde
CC       axonal long-range transport of presynaptic lysosome-related vesicles
CC       required for presynaptic biogenesis and synaptic function (By
CC       similarity). Also acts as a regulator of endosome to lysosome
CC       trafficking pathways of special significance for host defense
CC       (PubMed:21802320). Regulates cargo trafficking to lysosomes by binding
CC       to PLEKHM1 and recruiting the HOPS subunit VPS41, resulting in
CC       functional assembly of the HOPS complex on lysosomal membranes
CC       (PubMed:16537643, PubMed:25908847). Plays an important role in cargo
CC       delivery to lysosomes for antigen presentation and microbial killing.
CC       Directs the intersection of CD1d with lipid antigens in lysosomes, and
CC       plays a role in intersecting phagosomes with lysosomes to generate
CC       phagolysosomes that kill microbes (PubMed:25908847, PubMed:21802320).
CC       Involved in the process of MHC II presentation. Regulates the delivery
CC       of antigens to lysosomes and the formation of MHC II-peptide complexes
CC       through the recruitment of the HOPS complex to lysosomes allowing the
CC       fusion of late endosomes to lysosomes (By similarity). May play a role
CC       in chromosome segregation (PubMed:15331635).
CC       {ECO:0000250|UniProtKB:Q9CQW2, ECO:0000269|PubMed:15331635,
CC       ECO:0000269|PubMed:16537643, ECO:0000269|PubMed:16650381,
CC       ECO:0000269|PubMed:21802320, ECO:0000269|PubMed:22172677,
CC       ECO:0000269|PubMed:24088571, ECO:0000269|PubMed:25898167,
CC       ECO:0000269|PubMed:25908847, ECO:0000269|PubMed:27808481,
CC       ECO:0000269|PubMed:28325809, ECO:0000269|PubMed:29592961}.
CC   -!- FUNCTION: (Microbial infection) During Mycobacterium tuberculosis (Mtb)
CC       infection, is required for plasma membrane repair by controlling the
CC       exocytosis of lysosomes in macrophages. ARL8B secretion pathway is
CC       crucial to control the type of cell death of the M. tuberculosis-
CC       infected macrophages, distinguishing avirulent from virulent Mtb
CC       induced necrotic cell death. {ECO:0000269|PubMed:29592961}.
CC   -!- FUNCTION: (Microbial infection) During infection, coronaviruses such as
CC       SARS-CoV-2 and the chaperone HSPA5/GRP78 are probably co-released
CC       through ARL8B-dependent lysosomal exocytic pathway for unconventional
CC       egress. {ECO:0000269|PubMed:33157038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000269|PubMed:15331635, ECO:0000269|PubMed:16537643};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000269|PubMed:15331635, ECO:0000269|PubMed:16537643};
CC   -!- SUBUNIT: Interacts with tubulin (PubMed:15331635, Ref.25). Interacts
CC       with BORCS5; recruits ARL8B to lysosomes (PubMed:25898167). Interacts
CC       with VPS41; the interaction mediates the recruitment of the HOPS
CC       complex to lysosomes (PubMed:21802320, PubMed:25908847). Interacts
CC       (GTP-bound form) with PLEKHM2 (via RUN domain); the interaction is
CC       required to recruit the motor protein kinesin-1 on lysosomes
CC       (PubMed:22172677, PubMed:28325809). Interacts (GTP-bound form) with
CC       PLEKHM1 (via RUN domain); the interaction is required for PLEKHM1
CC       localization to lysosomes and for ARL8B function in delivery and
CC       degradation of endocytic and autophagic cargo in lysosomes
CC       (PubMed:28325809). PLEKHM1 and PLEKHM2 compete for interaction with
CC       ARL8B (PubMed:28325809). {ECO:0000269|PubMed:15331635,
CC       ECO:0000269|PubMed:21802320, ECO:0000269|PubMed:22172677,
CC       ECO:0000269|PubMed:25898167, ECO:0000269|PubMed:25908847,
CC       ECO:0000269|PubMed:28325809, ECO:0000269|Ref.25}.
CC   -!- INTERACTION:
CC       Q9NVJ2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-718376, EBI-7062247;
CC       Q9NVJ2; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-718376, EBI-10262251;
CC       Q9NVJ2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-718376, EBI-8638294;
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000269|PubMed:16537643}. Lysosome membrane
CC       {ECO:0000269|PubMed:16650381, ECO:0000269|PubMed:21802320,
CC       ECO:0000269|PubMed:22172677, ECO:0000269|PubMed:25898167,
CC       ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:28325809,
CC       ECO:0000269|PubMed:29592961}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:15331635}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9CQW2}. Synapse {ECO:0000250|UniProtKB:Q9CQW2}.
CC       Cytolytic granule membrane {ECO:0000269|PubMed:24088571}. Note=GTP-
CC       bound form resides on lysosomal membranes, whereas GDP-bound form is
CC       likely associated with microtubular structures (PubMed:16650381).
CC       Localizes with microtubules at the spindle mid-zone during mitosis. In
CC       dendritic cells, localizes to MHC II+ compartments (By similarity).
CC       {ECO:0000250|UniProtKB:Q9CQW2, ECO:0000269|PubMed:15331635,
CC       ECO:0000269|PubMed:16650381}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NVJ2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NVJ2-2; Sequence=VSP_056238;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:15331635}.
CC   -!- PTM: Ubiquitinated at Lys-141 by RNF167, leading to its degradation.
CC       {ECO:0000269|PubMed:27808481}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; AB118751; BAD23992.1; -; mRNA.
DR   EMBL; AK001564; BAA91759.1; -; mRNA.
DR   EMBL; AK295465; BAG58397.1; -; mRNA.
DR   EMBL; CR457264; CAG33545.1; -; mRNA.
DR   EMBL; AC021999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW63919.1; -; Genomic_DNA.
DR   EMBL; BC013131; AAH13131.1; -; mRNA.
DR   EMBL; BC063125; AAH63125.1; -; mRNA.
DR   CCDS; CCDS2566.1; -. [Q9NVJ2-1]
DR   RefSeq; NP_060654.1; NM_018184.2. [Q9NVJ2-1]
DR   PDB; 2AL7; X-ray; 1.85 A; A=18-184.
DR   PDBsum; 2AL7; -.
DR   AlphaFoldDB; Q9NVJ2; -.
DR   SMR; Q9NVJ2; -.
DR   BioGRID; 120503; 176.
DR   IntAct; Q9NVJ2; 35.
DR   MINT; Q9NVJ2; -.
DR   STRING; 9606.ENSP00000256496; -.
DR   ChEMBL; CHEMBL4295962; -.
DR   GlyGen; Q9NVJ2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NVJ2; -.
DR   PhosphoSitePlus; Q9NVJ2; -.
DR   SwissPalm; Q9NVJ2; -.
DR   BioMuta; ARL8B; -.
DR   DMDM; 74752996; -.
DR   EPD; Q9NVJ2; -.
DR   jPOST; Q9NVJ2; -.
DR   MassIVE; Q9NVJ2; -.
DR   MaxQB; Q9NVJ2; -.
DR   PaxDb; Q9NVJ2; -.
DR   PeptideAtlas; Q9NVJ2; -.
DR   PRIDE; Q9NVJ2; -.
DR   ProteomicsDB; 4283; -.
DR   ProteomicsDB; 82817; -. [Q9NVJ2-1]
DR   TopDownProteomics; Q9NVJ2-1; -. [Q9NVJ2-1]
DR   Antibodypedia; 25235; 164 antibodies from 24 providers.
DR   DNASU; 55207; -.
DR   Ensembl; ENST00000256496.8; ENSP00000256496.3; ENSG00000134108.14. [Q9NVJ2-1]
DR   Ensembl; ENST00000419534.2; ENSP00000402996.2; ENSG00000134108.14. [Q9NVJ2-2]
DR   GeneID; 55207; -.
DR   KEGG; hsa:55207; -.
DR   MANE-Select; ENST00000256496.8; ENSP00000256496.3; NM_018184.3; NP_060654.1.
DR   UCSC; uc003bqg.4; human. [Q9NVJ2-1]
DR   CTD; 55207; -.
DR   DisGeNET; 55207; -.
DR   GeneCards; ARL8B; -.
DR   HGNC; HGNC:25564; ARL8B.
DR   HPA; ENSG00000134108; Low tissue specificity.
DR   MIM; 616596; gene.
DR   neXtProt; NX_Q9NVJ2; -.
DR   OpenTargets; ENSG00000134108; -.
DR   PharmGKB; PA134959531; -.
DR   VEuPathDB; HostDB:ENSG00000134108; -.
DR   eggNOG; KOG0075; Eukaryota.
DR   GeneTree; ENSGT00940000154861; -.
DR   HOGENOM; CLU_040729_10_0_1; -.
DR   InParanoid; Q9NVJ2; -.
DR   OMA; SASWLWQ; -.
DR   PhylomeDB; Q9NVJ2; -.
DR   TreeFam; TF105470; -.
DR   PathwayCommons; Q9NVJ2; -.
DR   SignaLink; Q9NVJ2; -.
DR   BioGRID-ORCS; 55207; 42 hits in 1078 CRISPR screens.
DR   ChiTaRS; ARL8B; human.
DR   EvolutionaryTrace; Q9NVJ2; -.
DR   GeneWiki; ARL8B; -.
DR   GenomeRNAi; 55207; -.
DR   Pharos; Q9NVJ2; Tbio.
DR   PRO; PR:Q9NVJ2; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9NVJ2; protein.
DR   Bgee; ENSG00000134108; Expressed in middle temporal gyrus and 207 other tissues.
DR   ExpressionAtlas; Q9NVJ2; baseline and differential.
DR   Genevisible; Q9NVJ2; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0101004; C:cytolytic granule membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR   GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR   GO; GO:0002747; P:antigen processing and presentation following phagocytosis; IMP:UniProtKB.
DR   GO; GO:0002505; P:antigen processing and presentation of polysaccharide antigen via MHC class II; ISS:UniProtKB.
DR   GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:UniProtKB.
DR   GO; GO:1990927; P:calcium ion regulated lysosome exocytosis; IMP:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0016197; P:endosomal transport; IEA:Ensembl.
DR   GO; GO:0090117; P:endosome to lysosome transport of low-density lipoprotein particle; IMP:UniProtKB.
DR   GO; GO:1902774; P:late endosome to lysosome transport; IMP:UniProtKB.
DR   GO; GO:0032418; P:lysosome localization; IDA:UniProtKB.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:UniProtKB.
DR   GO; GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB.
DR   GO; GO:0001778; P:plasma membrane repair; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0046754; P:viral exocytosis; IMP:UniProtKB.
DR   CDD; cd04159; Arl10_like; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR044154; Arl8a/8b.
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; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Endosome; GTP-binding; Hydrolase; Isopeptide bond; Lysosome; Membrane;
KW   Nucleotide-binding; Protein transport; Reference proteome; Synapse;
KW   Transport; Ubl conjugation.
FT   CHAIN           1..186
FT                   /note="ADP-ribosylation factor-like protein 8B"
FT                   /id="PRO_0000232921"
FT   INTRAMEM        1..19
FT                   /note="Note=Mediates targeting to membranes"
FT                   /evidence="ECO:0000269|PubMed:16537643"
FT   BINDING         29..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.25"
FT   BINDING         71..75
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62330"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.25"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:16537643,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   CROSSLNK        141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:27808481"
FT   VAR_SEQ         125..186
FT                   /note="VLVLGNKRDLPNALDEKQLIEKMNLSAIQDREICCYSISCKEKDNIDITLQW
FT                   LIQHSKSRRS -> ISHFSGLFSIQNLEEAEASPEVFQSFLAIILELLSVPLK (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056238"
FT   MUTAGEN         2
FT                   /note="L->A: Diffuse cytoplasmic distribution and loss of
FT                   localization to lysosomes. No effect on acetylation."
FT                   /evidence="ECO:0000269|PubMed:16537643"
FT   MUTAGEN         2
FT                   /note="L->F: No effect on localization and acetylation."
FT                   /evidence="ECO:0000269|PubMed:16537643"
FT   MUTAGEN         5..12
FT                   /note="ISRLLDWF->ASRALDWA: Diffuse cytoplasmic distribution
FT                   and loss of localization to lysosomes. No effect on
FT                   acetylation."
FT                   /evidence="ECO:0000269|PubMed:16537643"
FT   MUTAGEN         34
FT                   /note="T->N: Preferentially binds GDP. Alters chromosome
FT                   segregation. Decreases interaction with VPS41. Loss of
FT                   lysosomal location. Loss of interaction with PLEKHM1."
FT                   /evidence="ECO:0000269|PubMed:15331635,
FT                   ECO:0000269|PubMed:16650381, ECO:0000269|PubMed:21802320"
FT   MUTAGEN         49..58
FT                   /note="Missing: Alters chromosome segregation."
FT                   /evidence="ECO:0000269|PubMed:15331635"
FT   MUTAGEN         70
FT                   /note="W->R: Preferentially binds GTP."
FT                   /evidence="ECO:0000269|PubMed:15331635"
FT   MUTAGEN         74..85
FT                   /note="Missing: Alters chromosome segregation."
FT                   /evidence="ECO:0000269|PubMed:15331635"
FT   MUTAGEN         75
FT                   /note="Q->L: Prevents GTP hydrolysis. No effect on
FT                   lysosomal location. Alters lysosomes cellular distribution
FT                   and motility. Increases interaction with VPS41. No effect
FT                   on interaction with PLEKHM1."
FT                   /evidence="ECO:0000269|PubMed:16537643,
FT                   ECO:0000269|PubMed:16650381, ECO:0000269|PubMed:21802320,
FT                   ECO:0000269|PubMed:28325809"
FT   MUTAGEN         130
FT                   /note="N->I: Loss of GTP/GDP-binding. Affects chromosome
FT                   segregation."
FT                   /evidence="ECO:0000269|PubMed:15331635"
FT   MUTAGEN         141
FT                   /note="K->R: Abolished ubiquitination by RNF167."
FT                   /evidence="ECO:0000269|PubMed:27808481"
FT   STRAND          19..26
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           33..40
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           76..81
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           82..86
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           104..115
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           140..146
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   TURN            164..167
FT                   /evidence="ECO:0007829|PDB:2AL7"
FT   HELIX           170..178
FT                   /evidence="ECO:0007829|PDB:2AL7"
SQ   SEQUENCE   186 AA;  21539 MW;  5030B01AFD749223 CRC64;
     MLALISRLLD WFRSLFWKEE MELTLVGLQY SGKTTFVNVI ASGQFSEDMI PTVGFNMRKV
     TKGNVTIKIW DIGGQPRFRS MWERYCRGVN AIVYMIDAAD REKIEASRNE LHNLLDKPQL
     QGIPVLVLGN KRDLPNALDE KQLIEKMNLS AIQDREICCY SISCKEKDNI DITLQWLIQH
     SKSRRS
 
 
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