EXOC2_HUMAN
ID EXOC2_HUMAN Reviewed; 924 AA.
AC Q96KP1; B2RBE6; Q5JPC8; Q96AN6; Q9NUZ8; Q9UJM7;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Exocyst complex component 2;
DE AltName: Full=Exocyst complex component Sec5;
GN Name=EXOC2; Synonyms=SEC5, SEC5L1;
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], TISSUE SPECIFICITY, INTERACTION WITH GNEFR, AND
RP FUNCTION.
RX PubMed=12459492; DOI=10.1016/s0014-5793(02)03677-3;
RA Sjoelinder M., Uhlmann J., Ponstingl H.;
RT "DelGEF, a homologue of the Ran guanine nucleotide exchange factor RanGEF,
RT binds to the exocyst component Sec5 and modulates secretion.";
RL FEBS Lett. 532:211-215(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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].
RC TISSUE=Lymph node;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Mammary gland;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
RA Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
RA Guha M., Sillibourne J., Doxsey S.J.;
RT "Centriolin anchoring of exocyst and SNARE complexes at the midbody is
RT required for secretory-vesicle-mediated abscission.";
RL Cell 123:75-87(2005).
RN [7]
RP INTERACTION WITH RALA AND RALB, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-11.
RX PubMed=18756269; DOI=10.1038/emboj.2008.166;
RA Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M.,
RA Camonis J.;
RT "Distinct roles of RalA and RalB in the progression of cytokinesis are
RT supported by distinct RalGEFs.";
RL EMBO J. 27:2375-2387(2008).
RN [8]
RP INTERACTION WITH RALB.
RX PubMed=19166349; DOI=10.1021/bi802129d;
RA Fenwick R.B., Prasannan S., Campbell L.J., Nietlispach D., Evetts K.A.,
RA Camonis J., Mott H.R., Owen D.;
RT "Solution structure and dynamics of the small GTPase RalB in its active
RT conformation: significance for effector protein binding.";
RL Biochemistry 48:2192-2206(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-454, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-432; SER-435;
RP THR-440 AND SER-888, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [12]
RP INVOLVEMENT IN NEDFACH, VARIANTS NEDFACH HIS-130; 437-ARG--THR-924 DEL AND
RP SER-580, CHARACTERIZATION OF VARIANTS NEDFACH HIS-130; 437-ARG--THR-924 DEL
RP AND SER-580, AND FUNCTION.
RX PubMed=32639540; DOI=10.1084/jem.20192040;
RA Van Bergen N.J., Ahmed S.M., Collins F., Cowley M., Vetro A., Dale R.C.,
RA Hock D.H., de Caestecker C., Menezes M., Massey S., Ho G., Pisano T.,
RA Glover S., Gusman J., Stroud D.A., Dinger M., Guerrini R., Macara I.G.,
RA Christodoulou J.;
RT "Mutations in the exocyst component EXOC2 cause severe defects in human
RT brain development.";
RL J. Exp. Med. 217:0-0(2020).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC {ECO:0000269|PubMed:12459492, ECO:0000269|PubMed:32639540}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1
CC (By similarity). Interacts with GNEFR/DELGEF; this interaction occurs
CC only in the presence of magnesium or manganese and is stimulated by
CC dCTP or GTP (PubMed:12459492). Interacts with RALA and RALB
CC (PubMed:18756269, PubMed:19166349, PubMed:12459492) (By similarity).
CC Interacts with ARL13B; regulates ARL13B localization to the cilium
CC membrane. {ECO:0000250|UniProtKB:O54921, ECO:0000250|UniProtKB:Q9D4H1,
CC ECO:0000269|PubMed:12459492, ECO:0000269|PubMed:18756269,
CC ECO:0000269|PubMed:19166349}.
CC -!- INTERACTION:
CC Q96KP1; Q9NV70: EXOC1; NbExp=6; IntAct=EBI-465715, EBI-1045313;
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000269|PubMed:16213214, ECO:0000269|PubMed:18756269}.
CC Note=Recruitment to the midbody does not require RALA, nor RALB
CC (PubMed:18756269). Colocalizes with CNTRL/centriolin at the midbody
CC ring (PubMed:16213214). {ECO:0000269|PubMed:16213214,
CC ECO:0000269|PubMed:18756269}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain and
CC placenta. {ECO:0000269|PubMed:12459492}.
CC -!- DOMAIN: Interacts with RALA through the TIG domain. {ECO:0000250}.
CC -!- DISEASE: Neurodevelopmental disorder with dysmorphic facies and
CC cerebellar hypoplasia (NEDFACH) [MIM:619306]: An autosomal recessive
CC disorder characterized by global developmental delay, intellectual
CC disability, facial dysmorphism, and abnormalities of the cerebellum
CC observed on brain imaging. Disease severity is variable. Some affected
CC individuals have poor overall growth with microcephaly, delayed
CC walking, spasticity, and poor or absent speech. Others may achieve more
CC significant developmental milestones. Additional variable
CC manifestations may include cardiac ventricular septal defect,
CC spasticity, cataracts, optic nerve hypoplasia, seizures, and joint
CC contractures. {ECO:0000269|PubMed:32639540}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91963.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ414403; CAC92092.1; -; mRNA.
DR EMBL; AK001888; BAA91963.1; ALT_INIT; mRNA.
DR EMBL; AK314628; BAG37193.1; -; mRNA.
DR EMBL; AL833213; CAI46189.1; -; mRNA.
DR EMBL; AL031770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016918; AAH16918.2; -; mRNA.
DR EMBL; BC080542; AAH80542.1; -; mRNA.
DR CCDS; CCDS34327.1; -.
DR RefSeq; NP_060773.3; NM_018303.5.
DR RefSeq; XP_016866507.1; XM_017011018.1.
DR RefSeq; XP_016866508.1; XM_017011019.1.
DR RefSeq; XP_016866509.1; XM_017011020.1.
DR RefSeq; XP_016866510.1; XM_017011021.1.
DR RefSeq; XP_016866511.1; XM_017011022.1.
DR RefSeq; XP_016866512.1; XM_017011023.1.
DR RefSeq; XP_016866513.1; XM_017011024.1.
DR AlphaFoldDB; Q96KP1; -.
DR SMR; Q96KP1; -.
DR BioGRID; 120887; 87.
DR ComplexPortal; CPX-4943; Exocyst, EXOC6 variant.
DR ComplexPortal; CPX-4944; Exocyst, EXOC6B variant.
DR CORUM; Q96KP1; -.
DR DIP; DIP-31795N; -.
DR IntAct; Q96KP1; 29.
DR MINT; Q96KP1; -.
DR STRING; 9606.ENSP00000230449; -.
DR TCDB; 1.F.2.1.2; the octameric exocyst (exocyst) family.
DR iPTMnet; Q96KP1; -.
DR PhosphoSitePlus; Q96KP1; -.
DR BioMuta; EXOC2; -.
DR DMDM; 24638219; -.
DR EPD; Q96KP1; -.
DR jPOST; Q96KP1; -.
DR MassIVE; Q96KP1; -.
DR MaxQB; Q96KP1; -.
DR PaxDb; Q96KP1; -.
DR PeptideAtlas; Q96KP1; -.
DR PRIDE; Q96KP1; -.
DR ProteomicsDB; 77097; -.
DR Antibodypedia; 24190; 149 antibodies from 27 providers.
DR DNASU; 55770; -.
DR Ensembl; ENST00000230449.9; ENSP00000230449.4; ENSG00000112685.14.
DR GeneID; 55770; -.
DR KEGG; hsa:55770; -.
DR MANE-Select; ENST00000230449.9; ENSP00000230449.4; NM_018303.6; NP_060773.3.
DR UCSC; uc003mtd.5; human.
DR CTD; 55770; -.
DR DisGeNET; 55770; -.
DR GeneCards; EXOC2; -.
DR HGNC; HGNC:24968; EXOC2.
DR HPA; ENSG00000112685; Low tissue specificity.
DR MIM; 615329; gene.
DR MIM; 619306; phenotype.
DR neXtProt; NX_Q96KP1; -.
DR OpenTargets; ENSG00000112685; -.
DR PharmGKB; PA134862170; -.
DR VEuPathDB; HostDB:ENSG00000112685; -.
DR eggNOG; KOG2347; Eukaryota.
DR GeneTree; ENSGT00390000010872; -.
DR HOGENOM; CLU_005811_0_0_1; -.
DR InParanoid; Q96KP1; -.
DR OMA; LFPDACG; -.
DR OrthoDB; 97000at2759; -.
DR PhylomeDB; Q96KP1; -.
DR TreeFam; TF105891; -.
DR PathwayCommons; Q96KP1; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-264876; Insulin processing.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; Q96KP1; -.
DR BioGRID-ORCS; 55770; 255 hits in 1084 CRISPR screens.
DR ChiTaRS; EXOC2; human.
DR GeneWiki; EXOC2; -.
DR GenomeRNAi; 55770; -.
DR Pharos; Q96KP1; Tbio.
DR PRO; PR:Q96KP1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96KP1; protein.
DR Bgee; ENSG00000112685; Expressed in middle temporal gyrus and 170 other tissues.
DR ExpressionAtlas; Q96KP1; baseline and differential.
DR Genevisible; Q96KP1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000145; C:exocyst; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; IMP:AgBase.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:UniProtKB.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR029175; EXOC2/Sec5.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR13043; PTHR13043; 1.
DR Pfam; PF15469; Sec5; 1.
DR Pfam; PF01833; TIG; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Disease variant; Exocytosis;
KW Intellectual disability; Neurodegeneration; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..924
FT /note="Exocyst complex component 2"
FT /id="PRO_0000118918"
FT DOMAIN 8..93
FT /note="IPT/TIG"
FT COILED 240..260
FT /evidence="ECO:0000255"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 454
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 130
FT /note="R -> H (in NEDFACH; unknown pathological
FT significance; no effect on protein abundance)"
FT /evidence="ECO:0000269|PubMed:32639540"
FT /id="VAR_085744"
FT VARIANT 195
FT /note="N -> T (in dbSNP:rs35600069)"
FT /id="VAR_048956"
FT VARIANT 437..924
FT /note="Missing (in NEDFACH; decreased protein abundance;
FT shows defective ARL13B cilium membrane localization)"
FT /evidence="ECO:0000269|PubMed:32639540"
FT /id="VAR_085745"
FT VARIANT 580
FT /note="L -> S (in NEDFACH; unknown pathological
FT significance; no effect on protein abundance)"
FT /evidence="ECO:0000269|PubMed:32639540"
FT /id="VAR_085746"
FT MUTAGEN 11
FT /note="T->A: Impaired cytokinesis. Loss of RALA-binding. No
FT change in localization to the midbody during cytokinesis."
FT /evidence="ECO:0000269|PubMed:18756269"
FT CONFLICT 19
FT /note="I -> K (in Ref. 2; BAG37193)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="L -> H (in Ref. 2; BAA91963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 924 AA; 104066 MW; 2234E463DE8B076F CRC64;
MSRSRQPPLV TGISPNEGIP WTKVTIRGEN LGTGPTDLIG LTICGHNCLL TAEWMSASKI
VCRVGQAKND KGDIIVTTKS GGRGTSTVSF KLLKPEKIGI LDQSAVWVDE MNYYDMRTDR
NKGIPPLSLR PANPLGIEIE KSKFSQKDLE MLFHGMSADF TSENFSAAWY LIENHSNTSF
EQLKMAVTNL KRQANKKSEG SLAYVKGGLS TFFEAQDALS AIHQKLEADG TEKVEGSMTQ
KLENVLNRAS NTADTLFQEV LGRKDKADST RNALNVLQRF KFLFNLPLNI ERNIQKGDYD
VVINDYEKAK SLFGKTEVQV FKKYYAEVET RIEALRELLL DKLLETPSTL HDQKRYIRYL
SDLHASGDPA WQCIGAQHKW ILQLMHSCKE GYVKDLKGNP GLHSPMLDLD NDTRPSVLGH
LSQTASLKRG SSFQSGRDDT WRYKTPHRVA FVEKLTKLVL SQLPNFWKLW ISYVNGSLFS
ETAEKSGQIE RSKNVRQRQN DFKKMIQEVM HSLVKLTRGA LLPLSIRDGE AKQYGGWEVK
CELSGQWLAH AIQTVRLTHE SLTALEIPND LLQTIQDLIL DLRVRCVMAT LQHTAEEIKR
LAEKEDWIVD NEGLTSLPCQ FEQCIVCSLQ SLKGVLECKP GEASVFQQPK TQEEVCQLSI
NIMQVFIYCL EQLSTKPDAD IDTTHLSVDV SSPDLFGSIH EDFSLTSEQR LLIVLSNCCY
LERHTFLNIA EHFEKHNFQG IEKITQVSMA SLKELDQRLF ENYIELKADP IVGSLEPGIY
AGYFDWKDCL PPTGVRNYLK EALVNIIAVH AEVFTISKEL VPRVLSKVIE AVSEELSRLM
QCVSSFSKNG ALQARLEICA LRDTVAVYLT PESKSSFKQA LEALPQLSSG ADKKLLEELL
NKFKSSMHLQ LTCFQAASST MMKT
