SEC16_PHANO
ID SEC16_PHANO Reviewed; 1776 AA.
AC Q0V3R6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=COPII coat assembly protein SEC16;
DE AltName: Full=Protein transport protein SEC16;
GN Name=SEC16; ORFNames=SNOG_01348;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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 -!- 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; CH445326; EAT90997.2; -; Genomic_DNA.
DR RefSeq; XP_001791990.1; XM_001791938.1.
DR AlphaFoldDB; Q0V3R6; -.
DR STRING; 13684.SNOT_01348; -.
DR EnsemblFungi; SNOT_01348; SNOT_01348; SNOG_01348.
DR GeneID; 5968835; -.
DR KEGG; pno:SNOG_01348; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_001147_1_0_1; -.
DR InParanoid; Q0V3R6; -.
DR OrthoDB; 56582at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1776
FT /note="COPII coat assembly protein SEC16"
FT /id="PRO_0000295541"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1776 AA; 188462 MW; 07D5E4B0D6C976B2 CRC64;
MDSDGVSHAP SVAQSAPSWN PALRHEKDHA PAATAKLPSQ VKPESSSEEE SEEEEEEEDD
DEDDEEEEDS DEDDDEEENA PAATAVSGPT PIAVLDGAQD SEDESESPSE LTKSTPIVQA
SQGSMEKRVE VIGAEEEALV NAAQALNISG NPATGQTKAE STDEAESDED SEEEESSDEE
AAAAGEHQAD NYEHQGEATA LEEAVNESVR VPLVDDAAPE SDDWGDSGDP FEIGGLQQDP
SLQTPHAEAA GTTVGDDVIG NTTVGGNAGD DLDWGNTEEE DFFGVVANKP VESVEPAQPT
QSPGAHVVQA QDAAPAKSEW DLDLDLDEDF LPDNEDGPVI ELSDDEGFLD DEPTAPVEQP
ASTGIGGASR YAPQAAQTSH SVASPYAAPG QFANPPQGSM TRSITTPAGG VYNGYGQNVA
YQQQQAARPT MPTSAQSYAD KSKGGYASPY DLPDDVVTTR KRTTPRPVIS ATQPAIPPPR
TSSMSSSSAP PRPLPPSNAS VASLSPPPSG HSMQGQMTGF PPAVPPKSAP PAKAPSSDFF
AELPVTSKPK PPGRYTPQPA AAAQSPSLQG PPQFTQKERT ASWSSLRNEV LPDTVGAQPH
LRQPEQLPMF PSQPSVPTRQ NSLPIPQSTA PPPSSRYSPA PPSVPANNAR YSPAPPTAQG
GANSRYSPAP PGSQGAAHAR YVSEPPTGPA RTPSQTYAPR TSSPLAFHST PHHQENTTNV
SEQQLPGHHV TQSADGVPRA PFRSPLEGVS EALELDSTSS DRPPTTARSD TPPPTRSSTS
SAIGSPRKKG NYTPQYQPMN PMAPSRSLSQ SPATGMKQPG PMYGAAPIAA SYGTHIQEAT
TTNSIPHRRQ ASLNYECIVP EDERAVDPLQ RYKGHPVFAW GLGGTIVTTF PKQIPRYGGG
MTAPMVKCSP GEIKIQSVKE IIPLAEDLAK FPGPLKAKSK KKDVLSWLTK RLESLELQIK
DPNTEHTLSV DELKRLEEKT LLLKLLQFLV ENDGRLEGEA ANAAFKNLFS PEADNASDAE
GSFSTAADIV GRSRSNTVNT PAEPIDARAI EDLQKMLARG EREKAVWHAV DQRLWGHAML
LSSTLSKDIW KQVVQEFVRN EVKKVGRSNQ ALAVLYEVFA GNHEDCIDEL VPASARAGFQ
MVSTDGAGAA LNAQQGLDKW RETIALILNN RSEGDVSALL SLGKLLSQYG RVEAAHICFI
LGRSVAHVSG VDDALADLVL IGIDHKQHPT ELGVDLEPIL LTEVYEFALS LSAQVNSHIM
PHLQNYKLAH AYQLAEHGYR TEAQAYCDAI AAAMKATTRT SPYYNLSFIA SLDDLSKRLS
QSPKDSSSSW ISKPSMDRVS TSLMSKFNSF IAGEDDGPSS NAATGTEVGP FAKITGDSPG
LTPSHSNADL YADCFCKFKI CSFKYIRTKD VIRATEIALR AAGQTFYGVE RQPPPQPQLS
PPSQRTQAKM QSYSPLRAEH NVSQPSYGNP YMPTPPNEET ASASSFGGYQ PQQGTGHSFD
DPAPPTSSFD EPSYQPYNPD ADDMEEDNKP KKKSIMDDDD DDLVARAAAL KIGSGSNSKS
DADKKADEAF RKAAEADAKR DKENAAKKAG GGWLSGWFKK DPNAAPGPIK AKLGEESSFY
YDPDLGKWVN KKGGSSEPER ATATPPPPKG PPMGARSASG GMPPPSGPPP SGAGLMKPPT
SAPLRSSSMP PPMGLPGSRS STPGLPSDNE GGPKPPTLAR PSFGAASGPP SRPGTGMSNA
SSIDDLLGAP QARKGAGAKK KKGGRYVDVF PQGQAS
