SC161_CAEEL
ID SC161_CAEEL Reviewed; 1232 AA.
AC P34643; M1ZK05;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein transport protein sec-16A.1 {ECO:0000305};
DE AltName: Full=Secretory cargo traffic protein sec-16A.1 {ECO:0000305};
GN Name=sec-16A.1 {ECO:0000312|WormBase:ZK512.5a};
GN Synonyms=sec-16 {ECO:0000303|PubMed:21478858,
GN ECO:0000312|WormBase:ZK512.5a};
GN ORFNames=ZK512.5 {ECO:0000312|WormBase:ZK512.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH TFG-1,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21478858; DOI=10.1038/ncb2225;
RA Witte K., Schuh A.L., Hegermann J., Sarkeshik A., Mayers J.R., Schwarze K.,
RA Yates J.R. III, Eimer S., Audhya A.;
RT "TFG-1 function in protein secretion and oncogenesis.";
RL Nat. Cell Biol. 13:550-558(2011).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=23840591; DOI=10.1371/journal.pone.0067076;
RA Ackema K.B., Sauder U., Solinger J.A., Spang A.;
RT "The ArfGEF GBF-1 Is Required for ER Structure, Secretion and Endocytic
RT Transport in C. elegans.";
RL PLoS ONE 8:e67076-e67076(2013).
CC -!- FUNCTION: Plays a role in the organization of the endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER) (PubMed:21478858). In association with tfg-1, accumulates at ERES
CC to positively regulate secretory cargo trafficking from the endoplasmic
CC reticulum to the endoplasmic reticulum-Golgi intermediate compartment
CC (ERGIC) and Golgi apparatus (PubMed:21478858).
CC {ECO:0000269|PubMed:21478858}.
CC -!- SUBUNIT: Interacts with tfg-1 (via N-terminus); the interaction is
CC direct and is required for both the localization of tfg-1 and to
CC maintain the distribution of sec-16A.1 at endoplasmic reticulum exit
CC sites (ERES). {ECO:0000269|PubMed:21478858}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:21478858}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:23840591}. Note=Co-localizes with tfg-1
CC at endoplasmic reticulum exit sites (ERES).
CC {ECO:0000269|PubMed:21478858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:ZK512.5a};
CC IsoId=P34643-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:ZK512.5b};
CC IsoId=P34643-2; Sequence=VSP_053667;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown abolishes localization of
CC tfg-1 to endoplasmic reticulum exit sites (ERES).
CC {ECO:0000269|PubMed:21478858}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
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DR EMBL; BX284603; CAA80146.1; -; Genomic_DNA.
DR EMBL; BX284603; CCU83371.1; -; Genomic_DNA.
DR PIR; S40766; S40766.
DR RefSeq; NP_001293651.1; NM_001306722.1. [P34643-2]
DR RefSeq; NP_499022.1; NM_066621.4. [P34643-1]
DR AlphaFoldDB; P34643; -.
DR BioGRID; 41488; 27.
DR DIP; DIP-25929N; -.
DR IntAct; P34643; 7.
DR STRING; 6239.ZK512.5a; -.
DR iPTMnet; P34643; -.
DR EPD; P34643; -.
DR PaxDb; P34643; -.
DR PeptideAtlas; P34643; -.
DR EnsemblMetazoa; ZK512.5a.1; ZK512.5a.1; WBGene00013985. [P34643-1]
DR EnsemblMetazoa; ZK512.5b.1; ZK512.5b.1; WBGene00013985. [P34643-2]
DR GeneID; 176289; -.
DR KEGG; cel:CELE_ZK512.5; -.
DR UCSC; ZK512.5; c. elegans. [P34643-1]
DR CTD; 176289; -.
DR WormBase; ZK512.5a; CE00411; WBGene00013985; sec-16A.1. [P34643-1]
DR WormBase; ZK512.5b; CE48211; WBGene00013985; sec-16A.1. [P34643-2]
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_257407_0_0_1; -.
DR InParanoid; P34643; -.
DR OMA; TDIFDYA; -.
DR OrthoDB; 292716at2759; -.
DR Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR SignaLink; P34643; -.
DR PRO; PR:P34643; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013985; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:WormBase.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:WormBase.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IMP:WormBase.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; ER-Golgi transport;
KW Reference proteome; Transport.
FT CHAIN 1..1232
FT /note="Protein transport protein sec-16A.1"
FT /id="PRO_0000065519"
FT REGION 18..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1040
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053667"
SQ SEQUENCE 1232 AA; 134924 MW; 6DFC35D664AA8D6A CRC64;
MRRYRIDSMK YEQRMNAGAS GFDMSDWNNP YNASPPSSRG GDDDASSVNH SRPRRSRLDN
DIPQPRRPIL IQPARPVSQK SNRQGTGMSN GSRGLNSTFN GYDRTYSRYH QNSSRGPSEG
FSGAPSARNA SGYASDYANS RAGVGLLPNN HREPVRPRST AAERYANASS MRNGFVYDSG
ESDKTSEELE EDEEEEEVRN FYMEGRAQGS RSVTNTLASE VYNSESESYY YGVVKLGSAI
VDHVFRTMPP PEKYYKMPPI DRVAYVFYCA VNNKPYNNID EFHVIFNREF YSYRGYGDSK
DLALFKVCKR MQEEFSLKQL EADRLAYEKA RQEAAESEKL DFNQHKIEER EEPKLNISQP
EEVLSNGPLH YHSCLQFATI GVGGKLVIIK PAGTIDSITG HVLSTSSVHV DDLKTFLHFD
EQSGKVIESV QNFKGPLIAG QTPTHSVRLY IQRQIDALRQ IRNAGDVKKS EVVDALLVWQ
LLEIMVQQHG RVTGPDVATL LTNASEELGE KTGISSNGTS ESGSKFEAKE RFNKYLLGGH
INEAVESAIT DGLYADAMTL IRRLHPNDAK KIEEIEARFM NLRSIDDPFA TLVAVSSDQP
PPILTNSAFD DDNNWKRHAA IVLANLNSQT AMQTIYHLGL LLAKRERNCA ADFCLLVVCI
LAGYDPFIPV AHDGDETSRK HIGLVHSGSN LLNRVDGLSG TAGFSFTDLH ATDIFDYALR
LGNNNVDSPL AKSIDYQLAR IEYAKKLSSF GGFATDAFRY CTEVARSLWM YVAAFDKNAM
FDLCDLAESL QYMAAATPDE SGWITTMRGM LGAAPVQESQ QHVPQPQPVE NKSISSEAKK
WHDEHQAPLE IGSRNDQQHN DKTVEKPIAP GRASLPPPTL VTESSSESTF TDKSDSSVTV
AASASRTSTL TSSTLPPPPS LPKTIEKPIS TPPPISKNVV PEMTPPAIVK PPMPTLSMPI
PPVSTPIMVS PQPIPIPKPV DASIAKSPRS ELDDLWDTSP PSNQTSYPPA PRNIQPSYSP
APNFANPTAP SVPTPPPAVS SAPVLQQATL GQASIPNAKT TAPPVPQKQP ELALNERKAS
KGWFGSIKEK VIKSIPSANQ MILPDDSKPS IVWDPVQKRY VGAGVEEEVV AAPPPVMSAP
HLMGGGPDSN KSSTNSLRSA RSGVGSRYLQ SGMATSQAPA MDTGMPPMMP PTMPMSFSFM
PAPTEDDSSE YVDPFSGEPT APSESLSKQN ND
