RIPL1_HUMAN
ID RIPL1_HUMAN Reviewed; 403 AA.
AC Q5EBL4; Q66K36; Q8N1M0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=RILP-like protein 1;
DE AltName: Full=Rab-interacting lysosomal-like protein 1;
GN Name=RILPL1; Synonyms=RLP1;
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 2).
RC TISSUE=Pericardium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Chondrosarcoma;
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 LACK OF FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14668488; DOI=10.1091/mbc.e03-06-0413;
RA Wang T., Wong K.K., Hong W.;
RT "A unique region of RILP distinguishes it from its related proteins in its
RT regulation of lysosomal morphology and interaction with Rab7 and Rab34.";
RL Mol. Biol. Cell 15:815-826(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
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 [9]
RP INTERACTION WITH RAB8A; RAB10 AND RAB12, AND MUTAGENESIS OF ARG-291;
RP ARG-293; ARG-300; LYS-310 AND LYS-324.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [10]
RP FUNCTION, INTERACTION WITH RAB8A AND RAB10, AND SUBCELLULAR LOCATION.
RX PubMed=30398148; DOI=10.7554/elife.40202;
RA Dhekne H.S., Yanatori I., Gomez R.C., Tonelli F., Diez F., Schuele B.,
RA Steger M., Alessi D.R., Pfeffer S.R.;
RT "A pathway for Parkinson's Disease LRRK2 kinase to block primary cilia and
RT Sonic hedgehog signaling in the brain.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Plays a role in the regulation of cell shape and polarity (By
CC similarity). Plays a role in cellular protein transport, including
CC protein transport away from primary cilia (By similarity).
CC Neuroprotective protein, which acts by sequestring GAPDH in the cytosol
CC and prevent the apoptotic function of GAPDH in the nucleus (By
CC similarity). Competes with SIAH1 for binding GAPDH (By similarity).
CC Does not regulate lysosomal morphology and distribution
CC (PubMed:14668488). Binds to RAB10 following LRRK2-mediated RAB10
CC phosphorylation which leads to inhibition of ciliogenesis
CC (PubMed:30398148). {ECO:0000250|UniProtKB:D3ZUQ0,
CC ECO:0000250|UniProtKB:Q9JJC6, ECO:0000269|PubMed:14668488,
CC ECO:0000269|PubMed:30398148}.
CC -!- SUBUNIT: Interacts (when S-nitrosylated) with GAPDH (By similarity).
CC Interacts with RAB8A; interaction is dependent on the phosphorylation
CC of 'Thr-72' of RAB8A (PubMed:29125462, PubMed:30398148). Interacts with
CC RAB10 and RAB12; the interaction is dependent on the phosphorylation of
CC 'Thr-73' of RAB10, and 'Ser-105' of RAB12 (PubMed:29125462,
CC PubMed:30398148). {ECO:0000250|UniProtKB:D3ZUQ0,
CC ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30398148}.
CC -!- INTERACTION:
CC Q5EBL4; P61006: RAB8A; NbExp=2; IntAct=EBI-2797110, EBI-722293;
CC Q5EBL4-3; Q92624: APPBP2; NbExp=3; IntAct=EBI-12072024, EBI-743771;
CC Q5EBL4-3; O75425: MOSPD3; NbExp=3; IntAct=EBI-12072024, EBI-12179105;
CC Q5EBL4-3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12072024, EBI-741158;
CC Q5EBL4-3; Q86T03: PIP4P1; NbExp=5; IntAct=EBI-12072024, EBI-6164623;
CC Q5EBL4-3; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12072024, EBI-8652744;
CC Q5EBL4-3; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-12072024, EBI-765817;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14668488,
CC ECO:0000269|PubMed:30398148}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:30398148}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:30398148}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5EBL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5EBL4-2; Sequence=VSP_027606, VSP_027608;
CC Name=3;
CC IsoId=Q5EBL4-3; Sequence=VSP_027605, VSP_027607;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at lower level in liver
CC and kidney. {ECO:0000269|PubMed:14668488}.
CC -!- PTM: S-nitrosylation is required for the interaction with GAPDH.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
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DR EMBL; AK096697; BAC04845.1; -; mRNA.
DR EMBL; AC055713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC145423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080626; AAH80626.1; -; mRNA.
DR EMBL; BC089444; AAH89444.1; -; mRNA.
DR CCDS; CCDS45006.1; -. [Q5EBL4-1]
DR RefSeq; NP_001306172.1; NM_001319243.1.
DR RefSeq; NP_001306173.1; NM_001319244.1. [Q5EBL4-3]
DR RefSeq; NP_001306231.1; NM_001319302.1. [Q5EBL4-3]
DR RefSeq; NP_847884.2; NM_178314.4. [Q5EBL4-1]
DR AlphaFoldDB; Q5EBL4; -.
DR SMR; Q5EBL4; -.
DR BioGRID; 131631; 15.
DR IntAct; Q5EBL4; 12.
DR STRING; 9606.ENSP00000366070; -.
DR GlyGen; Q5EBL4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5EBL4; -.
DR PhosphoSitePlus; Q5EBL4; -.
DR BioMuta; RILPL1; -.
DR DMDM; 74736071; -.
DR EPD; Q5EBL4; -.
DR jPOST; Q5EBL4; -.
DR MassIVE; Q5EBL4; -.
DR MaxQB; Q5EBL4; -.
DR PaxDb; Q5EBL4; -.
DR PeptideAtlas; Q5EBL4; -.
DR PRIDE; Q5EBL4; -.
DR ProteomicsDB; 62761; -. [Q5EBL4-1]
DR ProteomicsDB; 62762; -. [Q5EBL4-2]
DR ProteomicsDB; 62763; -. [Q5EBL4-3]
DR Antibodypedia; 31816; 106 antibodies from 25 providers.
DR DNASU; 353116; -.
DR Ensembl; ENST00000376874.9; ENSP00000366070.4; ENSG00000188026.13. [Q5EBL4-1]
DR GeneID; 353116; -.
DR KEGG; hsa:353116; -.
DR MANE-Select; ENST00000376874.9; ENSP00000366070.4; NM_178314.5; NP_847884.2.
DR UCSC; uc001ufe.3; human. [Q5EBL4-1]
DR CTD; 353116; -.
DR DisGeNET; 353116; -.
DR GeneCards; RILPL1; -.
DR HGNC; HGNC:26814; RILPL1.
DR HPA; ENSG00000188026; Tissue enhanced (heart muscle, skeletal muscle).
DR MIM; 614092; gene.
DR neXtProt; NX_Q5EBL4; -.
DR OpenTargets; ENSG00000188026; -.
DR PharmGKB; PA162401302; -.
DR VEuPathDB; HostDB:ENSG00000188026; -.
DR eggNOG; ENOG502QR9G; Eukaryota.
DR GeneTree; ENSGT00940000157897; -.
DR HOGENOM; CLU_044133_3_0_1; -.
DR InParanoid; Q5EBL4; -.
DR OMA; NHELHGA; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; Q5EBL4; -.
DR TreeFam; TF313489; -.
DR PathwayCommons; Q5EBL4; -.
DR SignaLink; Q5EBL4; -.
DR BioGRID-ORCS; 353116; 24 hits in 1086 CRISPR screens.
DR ChiTaRS; RILPL1; human.
DR GenomeRNAi; 353116; -.
DR Pharos; Q5EBL4; Tbio.
DR PRO; PR:Q5EBL4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q5EBL4; protein.
DR Bgee; ENSG00000188026; Expressed in left ventricle myocardium and 169 other tissues.
DR ExpressionAtlas; Q5EBL4; baseline and differential.
DR Genevisible; Q5EBL4; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR GO; GO:1903445; P:protein transport from ciliary membrane to plasma membrane; ISS:UniProtKB.
DR GO; GO:1901214; P:regulation of neuron death; ISS:UniProtKB.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR021563; RILP_dimer.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR Pfam; PF11461; RILP; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Protein transport; Reference proteome;
KW S-nitrosylation; Transport.
FT CHAIN 1..403
FT /note="RILP-like protein 1"
FT /id="PRO_0000299310"
FT DOMAIN 10..97
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 291..356
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 254..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..258
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUQ0"
FT MOD_RES 47
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUQ0"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027605"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027606"
FT VAR_SEQ 152..153
FT /note="HE -> MT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027607"
FT VAR_SEQ 357..403
FT /note="FSFFSRDKKRLANTQRNVHIQESFGQWANTHRDDGYTEQGQEALQHL -> I
FT FTAIMPMVAAGLIIDDPTLQPVRRLVSLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027608"
FT MUTAGEN 291
FT /note="R->L,E: Loss of interaction with RAB8A and RAB10."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 293
FT /note="R->L,E: Loss of interaction with RAB8A."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 300
FT /note="R->L,E: No loss of interaction with RAB8A."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 310
FT /note="K->L,E: Loss of interaction with RAB8A."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 324
FT /note="K->L,E: No loss of interaction with RAB8A."
FT /evidence="ECO:0000269|PubMed:29125462"
SQ SEQUENCE 403 AA; 47108 MW; 907F7120DE1C8D29 CRC64;
MEEERGSALA AESALEKNVA ELTVMDVYDI ASLVGHEFER VIDQHGCEAI ARLMPKVVRV
LEILEVLVSR HHVAPELDEL RLELDRLRLE RMDRIEKERK HQKELELVED VWRGEAQDLL
SQIAQLQEEN KQLMTNLSHK DVNFSEEEFQ KHEGMSERER QVMKKLKEVV DKQRDEIRAK
DRELGLKNED VEALQQQQTR LMKINHDLRH RVTVVEAQGK ALIEQKVELE ADLQTKEQEM
GSLRAELGKL RERLQGEHSQ NGEEEPETEP VGEESISDAE KVAMDLKDPN RPRFTLQELR
DVLHERNELK SKVFLLQEEL AYYKSEEMEE ENRIPQPPPI AHPRTSPQPE SGIKRLFSFF
SRDKKRLANT QRNVHIQESF GQWANTHRDD GYTEQGQEAL QHL
