SEC16_SCHPO
ID SEC16_SCHPO Reviewed; 1995 AA.
AC O14029;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=COPII coat assembly protein sec16;
DE AltName: Full=Protein transport protein sec16;
GN Name=sec16; ORFNames=SPAC29B12.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIL1.
RX PubMed=20404563; DOI=10.4161/cc.9.9.11526;
RA Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A.,
RA Kovacikova I., Miadokova E., Ammerer G., Gregan J.;
RT "High-throughput knockout screen in Schizosaccharomyces pombe identifies a
RT novel gene required for efficient homolog disjunction during meiosis I.";
RL Cell Cycle 9:1802-1808(2010).
CC -!- FUNCTION: Involved in the initiation of assembly of the COPII coat
CC required for the formation of transport vesicles from the endoplasmic
CC reticulum (ER) and the selection of cargo molecules. Also involved in
CC autophagy (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with dil1. {ECO:0000269|PubMed:20404563}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16252.2; -; Genomic_DNA.
DR PIR; T38495; T38495.
DR RefSeq; NP_594985.1; NM_001020416.2.
DR AlphaFoldDB; O14029; -.
DR BioGRID; 279131; 3.
DR STRING; 4896.SPAC29B12.07.1; -.
DR iPTMnet; O14029; -.
DR MaxQB; O14029; -.
DR PaxDb; O14029; -.
DR PRIDE; O14029; -.
DR EnsemblFungi; SPAC29B12.07.1; SPAC29B12.07.1:pep; SPAC29B12.07.
DR GeneID; 2542678; -.
DR KEGG; spo:SPAC29B12.07; -.
DR PomBase; SPAC29B12.07; sec16.
DR VEuPathDB; FungiDB:SPAC29B12.07; -.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_236268_0_0_1; -.
DR InParanoid; O14029; -.
DR OMA; LERWKGA; -.
DR PhylomeDB; O14029; -.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR PRO; PR:O14029; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030127; C:COPII vesicle coat; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; ISO:PomBase.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; NAS:PomBase.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
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 Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1995
FT /note="COPII coat assembly protein sec16"
FT /id="PRO_0000076312"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1649..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1833..1871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1907
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1995 AA; 218090 MW; 1B7D05482A303628 CRC64;
MDIESDHEPK ESSVDLEGRH DSIRKSFEAD DIDVTDENTI FSTSRKEQST IEPMDSFVEN
NIANSSSQQS VSEIDIQLPS SEPKEGVKEE SNLIESNSLD NVQEINPQNT IGDKSAHTEE
ESSNDNLVKI TAGTIISDIM DEPVVDEDDK LSEEDLSKED LETTLKGDEN YSSSQKEIYD
NDETIPKPPS PEVEKIETST SVENAYITNS QYNDTLDMED QTSDLITTFE HENEDHEVHE
VPSIHGMEGT FETVNLTSEA GNEKEFNNDS VVLNTTPKEM QISSLDAVDK LEDKPVSNDN
IKANIESSTT VDRASSQLES ENNESTFFVH NQNSSGQHQT LDFVASKPVT DTPELSKENT
LVSSENLNDP KPNLPETEVD FGEPLEVEAP SFVVQNNSAV QPTTQKTSED STDLHTNEIP
NVAQPPSSFE KENNKDTSKL ENPDISSSPL SPTEDLFPND PEEENLFSAA LGLNSNTGSQ
PSETQSKPSI DPSESITVTD NQDSLLFSQL TNNALQAENA TKVSENTIND EELIDDSEFT
SLMSNFLESS TVQTNKYLPK SSASPPANAP IVSSDVHKNE NAGTARRAPQ SGAFVASKAK
YSSPYDLPEE IVQVAQQKRS VSQNYNRQYS FQPRPATPSN PPRSLPPPSG QVNAPMSQTP
NPISFAYQHG TPLATPTMRA NSFNSYPASS AEPIRRPATT TVGHTPNLYS PKTNTYNSRH
MAYEMTKSHI NVISPGPSLQ VNAPYTPTSG ELGNKVSNPT KEFVSTSSYA PAANTRNAII
REPGILSPLS PRVQPVLSRR ESIISMGSSA SSYVPLEIAP RPMSSLEHTM NSAMSPGNLQ
RTANLYKPMT TPNAYNIKNS NQRETKYPYQ PQAINYSEVT QPGSSSLPTS GEEANIIRSP
GFTPLAAQKD ATIYTPSHAQ ATLYGNMDNN DRDNEGIHDI LQSDMEPVLP PHNSAYHANA
PVSSHSEGLN NRLPISPLPP QLHKTGTPSH QHGFDTAETT AKQYAPSIPP NFNPNVSIDT
MTEGVALPSA TLDSDKSSLH KRSAELSRNN SPRPDFLPLP NQPLLHSNLH SPVSPVVDSN
EDSRLKFLST QRPAFSFGPC GTIVMAFSTP SGLYTTSGKG TKFIAGPIKI EKLGDVLTDE
YRHLKEFKGP YLASNGKVDK HGKAEAIEWL SKYIDRLNQS LEYDDKNITL KDKLLLLQCL
KMLLEVSDRK LIVEKLRPIL LPSFEIPEPC NTATSVQELI NPEINQDDSP IVASRYCTTS
FLHRFYEYLL SGNKDEALTY ALQQKQWPYA IIVAHSIDAK TFQGVVRTFC KSEVKESMLR
SGVGVNLQLS LQLMSDAHAS SMSEFSSSTS LLNLADQSQA SNALVAWKEL LYNIIANHYS
DQKEALRVLG TLLLQENRVY AAHLVYILSL SPDVCSNKSN SLFELVGLSK HNLYPSHDDL
FDVTQLTEVL ELVFNVYSEK TPVFFTHLVP YRLYEAEVLA EAGEVSAARK YCELIGNYLN
RVAKKSNNVD PGFVLRVRDL TQQILENSAG SEDISSSWLG RTVSRPRLDT VLSSLGSKFS
KFVAGDPNFD VMRPATVGPG PFGKVASQKN LTVQTNTNNA AMESFYSDRP TSSGPSYQNR
TPLTGQESMN MGVYSPYRRS TEIAENMSMD GNAYPYTPAS QENPYTPRHS QEDNASVLSQ
QPLTFYSNVA DNSYMPVSAS QEPKMGMGTA FNMPTNEVHG VGAEMASPYQ PLQPASAHLP
NLQPTLAPIN QNAYVPSNIA PAMGAMQSAP SAEAVAAPSE SLNLNKDRSQ QAKQAAAQNV
ADLVRQEEEK EKQKQKAKKN AESGKKGGAK GWFSKLLRRD ESKDQPTVYK AKLGEKSHLH
YDKELKRWVN DDGSDLSNQA APPPPPPMAL PKAGPPSAAP TSALPPAGPP AGATAISGNP
GMPAPVPLTG KETAVPLSSM PNAPPSVASN AKLPPASNNR KVDPLEDILQ AMPPPTTRKA
RGKTSKRYVD VMRNS
