TPC6A_HUMAN
ID TPC6A_HUMAN Reviewed; 159 AA.
AC O75865; K7ERB1; K7ERQ4; Q9BQ45; Q9P092;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Trafficking protein particle complex subunit 6A {ECO:0000303|PubMed:19416478};
DE Short=TRAPP complex subunit 6A;
GN Name=TRAPPC6A {ECO:0000303|PubMed:19416478, ECO:0000312|HGNC:HGNC:23069};
GN ORFNames=HSPC289;
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 1).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 SUBUNIT, AND INTERACTION WITH TRAPPC3.
RX PubMed=16828797; DOI=10.1016/j.jmb.2006.06.012;
RA Kummel D., Muller J.J., Roske Y., Henke N., Heinemann U.;
RT "Structure of the Bet3-Tpc6B core of TRAPP: two Tpc6 paralogs form trimeric
RT complexes with Bet3 and Mum2.";
RL J. Mol. Biol. 361:22-32(2006).
RN [5]
RP IDENTIFICATION IN TRAPP COMPLEX, AND INTERACTION WITH TRAPPC2L.
RX PubMed=19416478; DOI=10.1111/j.1600-0854.2009.00906.x;
RA Scrivens P.J., Shahrzad N., Moores A., Morin A., Brunet S., Sacher M.;
RT "TRAPPC2L is a novel, highly conserved TRAPP-interacting protein.";
RL Traffic 10:724-736(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH TRAPPC3.
RX PubMed=16262728; DOI=10.1111/j.1600-0854.2005.00352.x;
RA Kim M.-S., Yi M.-J., Lee K.-H., Wagner J., Munger C., Kim Y.-G.,
RA Whiteway M., Cygler M., Oh B.-H., Sacher M.;
RT "Biochemical and crystallographic studies reveal a specific interaction
RT between TRAPP subunits Trs33p and Bet3p.";
RL Traffic 6:1183-1195(2005).
CC -!- FUNCTION: May play a role in vesicular transport during the biogenesis
CC of melanosomes. {ECO:0000250|UniProtKB:Q78XR0}.
CC -!- SUBUNIT: Part of the multisubunit transport protein particle (TRAPP)
CC complex. Heterodimer with TRAPPC3 (PubMed:16828797, PubMed:16262728).
CC The heterodimer TRAPPC3-TRAPPC6A interacts with TRAPPC2L. Interacts
CC with TRAPPC2L (PubMed:19416478). {ECO:0000269|PubMed:16262728,
CC ECO:0000269|PubMed:16828797, ECO:0000269|PubMed:19416478}.
CC -!- INTERACTION:
CC O75865; V9HW27: HEL-S-101; NbExp=3; IntAct=EBI-743573, EBI-10178933;
CC O75865; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-743573, EBI-747204;
CC O75865; Q96QF0: RAB3IP; NbExp=4; IntAct=EBI-743573, EBI-747844;
CC O75865; O43617: TRAPPC3; NbExp=9; IntAct=EBI-743573, EBI-743566;
CC O75865; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-743573, EBI-10182121;
CC O75865; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-743573, EBI-3957603;
CC O75865-2; O95429: BAG4; NbExp=3; IntAct=EBI-8451480, EBI-2949658;
CC O75865-2; O95810: CAVIN2; NbExp=3; IntAct=EBI-8451480, EBI-742141;
CC O75865-2; O95400: CD2BP2; NbExp=3; IntAct=EBI-8451480, EBI-768015;
CC O75865-2; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-8451480, EBI-751587;
CC O75865-2; O43281-2: EFS; NbExp=3; IntAct=EBI-8451480, EBI-11525448;
CC O75865-2; O00167-2: EYA2; NbExp=3; IntAct=EBI-8451480, EBI-12807776;
CC O75865-2; O15353: FOXN1; NbExp=3; IntAct=EBI-8451480, EBI-11319000;
CC O75865-2; Q9NZ52-2: GGA3; NbExp=3; IntAct=EBI-8451480, EBI-12075758;
CC O75865-2; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-8451480, EBI-2857315;
CC O75865-2; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-8451480, EBI-11163335;
CC O75865-2; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-8451480, EBI-739467;
CC O75865-2; Q9UJY1: HSPB8; NbExp=3; IntAct=EBI-8451480, EBI-739074;
CC O75865-2; Q9UKT9: IKZF3; NbExp=5; IntAct=EBI-8451480, EBI-747204;
CC O75865-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-8451480, EBI-6509505;
CC O75865-2; Q5T7N3: KANK4; NbExp=3; IntAct=EBI-8451480, EBI-9355810;
CC O75865-2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-8451480, EBI-11953846;
CC O75865-2; Q969G2: LHX4; NbExp=3; IntAct=EBI-8451480, EBI-2865388;
CC O75865-2; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-8451480, EBI-5662487;
CC O75865-2; P26367: PAX6; NbExp=3; IntAct=EBI-8451480, EBI-747278;
CC O75865-2; Q99471: PFDN5; NbExp=3; IntAct=EBI-8451480, EBI-357275;
CC O75865-2; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-8451480, EBI-11984839;
CC O75865-2; Q04864-2: REL; NbExp=3; IntAct=EBI-8451480, EBI-10829018;
CC O75865-2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-8451480, EBI-6257312;
CC O75865-2; Q9UIL1-3: SCOC; NbExp=3; IntAct=EBI-8451480, EBI-10692913;
CC O75865-2; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-8451480, EBI-748621;
CC O75865-2; Q9BWJ5: SF3B5; NbExp=3; IntAct=EBI-8451480, EBI-2555428;
CC O75865-2; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-8451480, EBI-12275818;
CC O75865-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-8451480, EBI-529518;
CC O75865-2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-8451480, EBI-11139477;
CC O75865-2; Q9UL33-2: TRAPPC2L; NbExp=5; IntAct=EBI-8451480, EBI-11119202;
CC O75865-2; O43617: TRAPPC3; NbExp=6; IntAct=EBI-8451480, EBI-743566;
CC O75865-2; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-8451480, EBI-17716262;
CC O75865-2; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-8451480, EBI-9090990;
CC O75865-2; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-8451480, EBI-2514383;
CC O75865-2; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-8451480, EBI-11419867;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75865-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75865-2; Sequence=VSP_019585;
CC Name=3;
CC IsoId=O75865-3; Sequence=VSP_047016;
CC Name=4;
CC IsoId=O75865-4; Sequence=VSP_047017;
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62259.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF28967.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF161407; AAF28967.1; ALT_INIT; mRNA.
DR EMBL; AC005757; AAC62259.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC001907; AAH01907.1; -; mRNA.
DR EMBL; BC004450; AAH04450.1; -; mRNA.
DR CCDS; CCDS12655.1; -. [O75865-2]
DR CCDS; CCDS59395.1; -. [O75865-4]
DR CCDS; CCDS59396.1; -. [O75865-3]
DR CCDS; CCDS59397.1; -. [O75865-1]
DR RefSeq; NP_001257820.1; NM_001270891.1. [O75865-1]
DR RefSeq; NP_001257821.1; NM_001270892.1. [O75865-4]
DR RefSeq; NP_001257822.1; NM_001270893.1. [O75865-3]
DR RefSeq; NP_077013.1; NM_024108.2. [O75865-2]
DR PDB; 2C0J; X-ray; 2.20 A; B=1-159.
DR PDB; 2J3T; X-ray; 2.40 A; B=1-159.
DR PDBsum; 2C0J; -.
DR PDBsum; 2J3T; -.
DR AlphaFoldDB; O75865; -.
DR SMR; O75865; -.
DR BioGRID; 122538; 57.
DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR CORUM; O75865; -.
DR DIP; DIP-37869N; -.
DR IntAct; O75865; 53.
DR MINT; O75865; -.
DR STRING; 9606.ENSP00000006275; -.
DR DrugBank; DB08342; S-palmitoyl-L-cysteine.
DR iPTMnet; O75865; -.
DR PhosphoSitePlus; O75865; -.
DR BioMuta; TRAPPC6A; -.
DR EPD; O75865; -.
DR jPOST; O75865; -.
DR MassIVE; O75865; -.
DR MaxQB; O75865; -.
DR PeptideAtlas; O75865; -.
DR PRIDE; O75865; -.
DR ProteomicsDB; 50231; -. [O75865-1]
DR ProteomicsDB; 50232; -. [O75865-2]
DR Antibodypedia; 49152; 138 antibodies from 26 providers.
DR DNASU; 79090; -.
DR Ensembl; ENST00000006275.8; ENSP00000006275.3; ENSG00000007255.10. [O75865-2]
DR Ensembl; ENST00000585934.1; ENSP00000468612.1; ENSG00000007255.10. [O75865-1]
DR Ensembl; ENST00000588062.5; ENSP00000468363.1; ENSG00000007255.10. [O75865-3]
DR Ensembl; ENST00000592647.1; ENSP00000468182.1; ENSG00000007255.10. [O75865-4]
DR GeneID; 79090; -.
DR KEGG; hsa:79090; -.
DR MANE-Select; ENST00000585934.1; ENSP00000468612.1; NM_001270891.2; NP_001257820.1.
DR UCSC; uc002pav.5; human. [O75865-1]
DR CTD; 79090; -.
DR DisGeNET; 79090; -.
DR GeneCards; TRAPPC6A; -.
DR HGNC; HGNC:23069; TRAPPC6A.
DR HPA; ENSG00000007255; Low tissue specificity.
DR MIM; 610396; gene.
DR neXtProt; NX_O75865; -.
DR OpenTargets; ENSG00000007255; -.
DR PharmGKB; PA134963625; -.
DR VEuPathDB; HostDB:ENSG00000007255; -.
DR eggNOG; KOG3316; Eukaryota.
DR GeneTree; ENSGT00390000012948; -.
DR HOGENOM; CLU_076409_3_1_1; -.
DR InParanoid; O75865; -.
DR OMA; QVVIQKA; -.
DR OrthoDB; 1566836at2759; -.
DR PhylomeDB; O75865; -.
DR TreeFam; TF313010; -.
DR PathwayCommons; O75865; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; O75865; -.
DR BioGRID-ORCS; 79090; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; TRAPPC6A; human.
DR EvolutionaryTrace; O75865; -.
DR GenomeRNAi; 79090; -.
DR Pharos; O75865; Tbio.
DR PRO; PR:O75865; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75865; protein.
DR Bgee; ENSG00000007255; Expressed in right uterine tube and 182 other tissues.
DR ExpressionAtlas; O75865; baseline and differential.
DR Genevisible; O75865; HS.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0030008; C:TRAPP complex; IBA:GO_Central.
DR GO; GO:1990072; C:TRAPPIII protein complex; IC:ComplexPortal.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:1903232; P:melanosome assembly; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR CDD; cd14944; TRAPPC6A_Trs33; 1.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR007194; TRAPP_component.
DR InterPro; IPR037992; TRAPPC6/Trs33.
DR PANTHER; PTHR12817; PTHR12817; 1.
DR Pfam; PF04051; TRAPP; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..159
FT /note="Trafficking protein particle complex subunit 6A"
FT /id="PRO_0000244539"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78XR0"
FT VAR_SEQ 28
FT /note="G -> GVSAGLRGEEAGATK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019585"
FT VAR_SEQ 29..159
FT /note="GQKMSLSVLEGMGFRVGQALGERLPRETLAFREELDVLKFLCKDLWVAVFQK
FT QMDSLRTNHQGTYVLQDNSFPLLLPMASGLQYLEEAPKFLAFTCGLLRGALYTLGIESV
FT VTASVAALPVCKFQVVIPKS -> AAPGDAGLQGGAGCPQVLVQRPVGGGVPEADGQPA
FT HQSPGDLRPARQQLPPPPPDGLWPAVSGGSTQVPGLHLRPPARRPLYPGH (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047016"
FT VAR_SEQ 29..159
FT /note="GQKMSLSVLEGMGFRVGQALGERLPRETLAFREELDVLKFLCKDLWVAVFQK
FT QMDSLRTNHQGTYVLQDNSFPLLLPMASGLQYLEEAPKFLAFTCGLLRGALYTLGIESV
FT VTASVAALPVCKFQVVIPKS -> VSAGLRGEEAGATKAAPGDAGLQGGAGCPQVLVQR
FT PVGGGVPEADGQPAHQSPGDLRPARQQLPPPPPDGLWPAVSGGSTQVPGLHLRPPARRP
FT LYPGH (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047017"
FT CONFLICT 99..123
FT /note="SFPLLLPMASGLQYLEEAPKFLAFT -> KLSPPPPDGLWPAVSGGSTQVPG
FT LH (in Ref. 1; AAF28967)"
FT /evidence="ECO:0000305"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2J3T"
FT HELIX 32..51
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:2C0J"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2C0J"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2C0J"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2C0J"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:2C0J"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:2C0J"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:2C0J"
SQ SEQUENCE 159 AA; 17605 MW; E7AF768013E7E031 CRC64;
MADTVLFEFL HTEMVAELWA HDPDPGPGGQ KMSLSVLEGM GFRVGQALGE RLPRETLAFR
EELDVLKFLC KDLWVAVFQK QMDSLRTNHQ GTYVLQDNSF PLLLPMASGL QYLEEAPKFL
AFTCGLLRGA LYTLGIESVV TASVAALPVC KFQVVIPKS
