ID   SEC16_COCIM             Reviewed;        1717 AA.
AC   Q1DHP3; J0HH29;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=COPII coat assembly protein SEC16;
DE   AltName: Full=Protein transport protein SEC16;
GN   Name=SEC16; ORFNames=CIMG_10170;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(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   -!- 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; GG704915; EAS27565.3; -; Genomic_DNA.
DR   RefSeq; XP_001239148.1; XM_001239147.2.
DR   AlphaFoldDB; Q1DHP3; -.
DR   STRING; 246410.Q1DHP3; -.
DR   EnsemblFungi; EAS27565; EAS27565; CIMG_10170.
DR   GeneID; 4558213; -.
DR   KEGG; cim:CIMG_10170; -.
DR   VEuPathDB; FungiDB:CIMG_10170; -.
DR   InParanoid; Q1DHP3; -.
DR   OMA; LERWKGA; -.
DR   OrthoDB; 56582at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:UniProt.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
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   InterPro; IPR024468; Sec16_N.
DR   PANTHER; PTHR13402; PTHR13402; 1.
DR   Pfam; PF12932; Sec16; 1.
DR   Pfam; PF12931; Sec16_C; 1.
DR   Pfam; PF12935; Sec16_N; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1717
FT                   /note="COPII coat assembly protein SEC16"
FT                   /id="PRO_0000295535"
FT   REGION          209..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1260..1505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1529..1564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1582..1717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..510
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..624
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1302..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1448..1479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1480..1505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1602..1622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1630..1653
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1673..1689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1717 AA;  184836 MW;  5B43B3E930494CFA CRC64;
     MAEDRVLGHE SGLFTDAIHL GAWNPAHRPE DFSDSVLHEV ATQTSVPIQT PDLAPCPPTE
     FELEHRDPEA SPPDNVLDET KDVEYLQAFP EAPTRLENSG HVDITGSEYM QSIEKTREGA
     VIDSNNGSPF IDSFKGSDDD TGTNTFPDDN IDFQAMIGQT HDDTRDVWDR STDAHVEDLS
     TQLVTEPYSA ENDKVNSWNS VFADDEGGGD FFSQISSQSK PTVAHLESEP RSDDMASHLS
     NGNVQPSNES QQTKAIDSLF QEDESTGEAD FFNSQGPAHV EPSLELLSET QPNSMPEDHP
     LPSLDPGKEL PHHQSVAVVQ DEKPEVIRPA EPGVAENLGE EELAERWKAF LGDDDILIEN
     ETLDGSIEGA NTHTAEYQRH PVQPASQVGS EQPPVNTYTP HQPSSSEMLG GLPAAGYSST
     LGNLTNPEKS KVESFSNQSK AGYQSPYDLP FDMRPKHAPP RKIAPPVGVN PPPRSSSMSG
     SRPPSSSYMV PGPNFSPVAA PPPVSGPDTT PPSTKEPVRT GSFFEELPVV SRSRPSTRGR
     YTPQPNMSQP ASNLPMAPVA PPPSLPQQSS DPYSQFQLQP PARLDPYSNL SAPPPQPAPT
     TSRYSPQPPP PGTKPAPFPR YSPAPPQSAC MTSSATYVSQ SPTVQSSVNA LPFQPRTSSP
     LAQHETAKSY PSPPRKRGSL PVTSIIPTSS VPQFGSDSQI VPPKRSMTQS PGRMMPLQSS
     VASNQNAYVR PASAHGSKSS IQAPLLQSAY APAANNRPTQ ALDFVVPTDG QEHDPLERWK
     GAPIFKFGFG GTLLSTFPKH IPRYATGQMT PRIKPTLGDI KTCPISQILP HNEPLDKFPG
     PLKSKSKKKD VLTWLSTMIS ALEGAPSTTD GHVDPVHQHR REDGILLWKV VRVLVEHDGA
     LRGSTAAEAS LQSIFSPGSM AMNSQFEYPS TGDSVSGSLK SESASSLGID VIHKSLVAGD
     RQKAVWDAVD HRLWGHAMLI SSTLDKSVWK QVTQEFIRRE VRSLGKNTES LAALYEIFAG
     NFEESIDELV PPSARAGLQM VSVHAGTGAP KDALEGLNKW RDTVNLILQN KIAQDHQALR
     ALGRLLASYG RVEASHICSL VAGTAAGPIF GDARDPQASI VLLGADHWRN PTTFMVEREA
     CLLTEVYEFA TSVLAASPSP SLAHLQAFKL RHAMYLAEEG HKSEAQQYCE AIVSIVTSKS
     NVKSPYYHQR FFAELDELSH RLRQAPTDGS SSWISKPSME KVSGSMWAKF NSFVSGDDNE
     VTSNGSGKGG DGDIGPFAKI AGTPPISRSP SVAEGHGSYF PSQPVAPSSS GSRYAPNSQY
     YAPYSSPEQS RGRRSLDAQR SPPQTAGRSY SQRRNSQDPS TPLEGNAYGS MPNHIYASPA
     TIGSHITPPQ ASHAPLAPVE EIYSPQIQSP TSEMPAIQTL PDGFGINQTG YMPLAEQVTR
     DDETNLKTTT TEQSGYQPPT YEPPSFSTGY EPPSYSANVE DNEHSDEEKP KKKSFMDDDD
     DDFMARAAQL RASEKEKMDR EAAEAFRKAA EADAKRPLAT EKKGWFSGWF GKKESGGAVR
     ADLGDENSFY FDKELNRWVN KKDPGSAATA AVTPPPPKSS APSSQSVSTS QTPTTPNLTN
     GRPGPSAVPG GTLSAPPPGI APLPTPPSSS LGPPSDSPRA IPRSVSAGAP TGPPSRPGTS
     LSNASSIDDL LGAPQARKGG TMKTRRKGRG YVDVMAK