EXC6B_HUMAN
ID EXC6B_HUMAN Reviewed; 811 AA.
AC Q9Y2D4; B8ZZY3;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Exocyst complex component 6B;
DE AltName: Full=Exocyst complex component Sec15B;
DE AltName: Full=SEC15-like protein 2;
GN Name=EXOC6B; Synonyms=KIAA0919, SEC15B, SEC15L2;
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=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 IDENTIFICATION AS EXOC6B.
RX PubMed=11406615; DOI=10.1074/jbc.c100320200;
RA Brymora A., Valova V.A., Larsen M.R., Roufogalis B.D., Robinson P.J.;
RT "The brain exocyst complex interacts with RalA in a GTP-dependent manner:
RT identification of a novel mammalian Sec3 gene and a second Sec15 gene.";
RL J. Biol. Chem. 276:29792-29797(2001).
RN [5]
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 [6]
RP INVOLVEMENT IN SEMDJL3, AND VARIANT SEMDJL3 302-TYR--SER-811 DEL.
RX PubMed=26669664; DOI=10.1038/ejhg.2015.261;
RA Girisha K.M., Kortuem F., Shah H., Alawi M., Dalal A., Bhavani G.S.,
RA Kutsche K.;
RT "A novel multiple joint dislocation syndrome associated with a homozygous
RT nonsense variant in the EXOC6B gene.";
RL Eur. J. Hum. Genet. 24:1206-1210(2016).
RN [7]
RP INVOLVEMENT IN SEMDJL3.
RX PubMed=30284759; DOI=10.1002/ajmg.a.40631;
RA Campos-Xavier B., Rogers R.C., Niel-Buetschi F., Ferreira C., Unger S.,
RA Spranger J., Superti-Furga A.;
RT "Confirmation of spondylo-epi-metaphyseal dysplasia with joint laxity,
RT EXOC6B type.";
RL Am. J. Med. Genet. A 176:2934-2935(2018).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC SEC10, SEC15, EXO70 and EXO84.
CC -!- INTERACTION:
CC Q9Y2D4; O00471: EXOC5; NbExp=6; IntAct=EBI-2690026, EBI-949824;
CC Q9Y2D4; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-2690026, EBI-12097232;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2D4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2D4-2; Sequence=VSP_040838, VSP_040839;
CC -!- DISEASE: Spondyloepimetaphyseal dysplasia with joint laxity, 3
CC (SEMDJL3) [MIM:618395]: An autosomal recessive bone disease
CC characterized by multiple joint dislocations at birth, severe joint
CC laxity, scoliosis, gracile metacarpals and metatarsals, delayed bone
CC age and poorly ossified carpal and tarsal bones.
CC {ECO:0000269|PubMed:26669664, ECO:0000269|PubMed:30284759}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the SEC15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76763.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023136; BAA76763.1; ALT_INIT; mRNA.
DR EMBL; AC006461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC160001; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS46333.1; -. [Q9Y2D4-1]
DR RefSeq; NP_056004.1; NM_015189.2. [Q9Y2D4-1]
DR AlphaFoldDB; Q9Y2D4; -.
DR SMR; Q9Y2D4; -.
DR BioGRID; 116838; 37.
DR ComplexPortal; CPX-4944; Exocyst, EXOC6B variant.
DR IntAct; Q9Y2D4; 16.
DR STRING; 9606.ENSP00000272427; -.
DR iPTMnet; Q9Y2D4; -.
DR PhosphoSitePlus; Q9Y2D4; -.
DR BioMuta; EXOC6B; -.
DR DMDM; 327478583; -.
DR EPD; Q9Y2D4; -.
DR jPOST; Q9Y2D4; -.
DR MassIVE; Q9Y2D4; -.
DR MaxQB; Q9Y2D4; -.
DR PaxDb; Q9Y2D4; -.
DR PeptideAtlas; Q9Y2D4; -.
DR PRIDE; Q9Y2D4; -.
DR ProteomicsDB; 85736; -. [Q9Y2D4-1]
DR ProteomicsDB; 85737; -. [Q9Y2D4-2]
DR Antibodypedia; 56922; 66 antibodies from 16 providers.
DR DNASU; 23233; -.
DR Ensembl; ENST00000272427.11; ENSP00000272427.7; ENSG00000144036.16. [Q9Y2D4-1]
DR GeneID; 23233; -.
DR KEGG; hsa:23233; -.
DR MANE-Select; ENST00000272427.11; ENSP00000272427.7; NM_015189.3; NP_056004.1.
DR UCSC; uc010fep.4; human. [Q9Y2D4-1]
DR CTD; 23233; -.
DR DisGeNET; 23233; -.
DR GeneCards; EXOC6B; -.
DR HGNC; HGNC:17085; EXOC6B.
DR HPA; ENSG00000144036; Tissue enhanced (heart).
DR MalaCards; EXOC6B; -.
DR MIM; 607880; gene.
DR MIM; 618395; phenotype.
DR neXtProt; NX_Q9Y2D4; -.
DR OpenTargets; ENSG00000144036; -.
DR Orphanet; 93359; Spondyloepimetaphyseal dysplasia with joint laxity.
DR PharmGKB; PA162385463; -.
DR VEuPathDB; HostDB:ENSG00000144036; -.
DR eggNOG; KOG2176; Eukaryota.
DR GeneTree; ENSGT00390000005739; -.
DR HOGENOM; CLU_009437_0_0_1; -.
DR InParanoid; Q9Y2D4; -.
DR OMA; MERACDF; -.
DR PhylomeDB; Q9Y2D4; -.
DR TreeFam; TF315199; -.
DR PathwayCommons; Q9Y2D4; -.
DR SignaLink; Q9Y2D4; -.
DR BioGRID-ORCS; 23233; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; EXOC6B; human.
DR GenomeRNAi; 23233; -.
DR Pharos; Q9Y2D4; Tbio.
DR PRO; PR:Q9Y2D4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y2D4; protein.
DR Bgee; ENSG00000144036; Expressed in calcaneal tendon and 171 other tissues.
DR ExpressionAtlas; Q9Y2D4; baseline and differential.
DR Genevisible; Q9Y2D4; HS.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
DR Gene3D; 1.10.357.30; -; 1.
DR Gene3D; 1.20.58.670; -; 1.
DR InterPro; IPR007225; EXOC6/Sec15.
DR InterPro; IPR042045; EXOC6/Sec15_C_dom1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR046361; Sec15_C.
DR PANTHER; PTHR12702; PTHR12702; 1.
DR Pfam; PF04091; Sec15; 1.
DR PIRSF; PIRSF025007; Sec15; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disease variant; Dwarfism; Exocytosis;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..811
FT /note="Exocyst complex component 6B"
FT /id="PRO_0000118954"
FT REGION 260..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..119
FT /evidence="ECO:0000255"
FT VAR_SEQ 661..672
FT /note="GKVAQTACMSAC -> VSGSCSYFVLYI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_040838"
FT VAR_SEQ 673..811
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_040839"
FT VARIANT 302..811
FT /note="Missing (in SEMDJL3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26669664"
FT /id="VAR_082175"
SQ SEQUENCE 811 AA; 94201 MW; A666EC6A0B82D9A2 CRC64;
MERGKMAEAE SLETAAEHER ILREIESTDT ACIGPTLRSV YDGEEHGRFM EKLETRIRNH
DREIEKMCNF HYQGFVDSIT ELLKVRGEAQ KLKNQVTDTN RKLQHEGKEL VIAMEELKQC
RLQQRNISAT VDKLMLCLPV LEMYSKLRDQ MKTKRHYPAL KTLEHLEHTY LPQVSHYRFC
KVMVDNIPKL REEIKDVSMS DLKDFLESIR KHSDKIGETA MKQAQQQRNL DNIVLQQPRI
GSKRKSKKDA YIIFDTEIES TSPKSEQDSG ILDVEDEEDD EEVPGAQDLV DFSPVYRCLH
IYSVLGARET FENYYRKQRR KQARLVLQPP SNMHETLDGY RKYFNQIVGF FVVEDHILHT
TQGLVNRAYI DELWEMALSK TIAALRTHSS YCSDPNLVLD LKNLIVLFAD TLQVYGFPVN
QLFDMLLEIR DQYSETLLKK WAGIFRNILD SDNYSPIPVT SEEMYKKVVG QFPFQDIELE
KQPFPKKFPF SEFVPKVYNQ IKEFIYACLK FSEDLHLSST EVDDMIRKST NLLLTRTLSN
SLQNVIKRKN IGLTELVQII INTTHLEKSC KYLEEFITNI TNVLPETVHT TKLYGTTTFK
DARHAAEEEI YTNLNQKIDQ FLQLADYDWM TGDLGNKASD YLVDLIAFLR STFAVFTHLP
GKVAQTACMS ACKHLATSLM QLLLEAEVRQ LTLGALQQFN LDVRECEQFA RSGPVPGFQE
DTLQLAFIDL RQLLDLFIQW DWSTYLADYG QPNCKYLRVN PVTALTLLEK MKDTSRKNNM
FAQFRKNERD KQKLIDTVAK QLRGLISSHH S
