ID   SEC16_EMENI             Reviewed;        1947 AA.
AC   Q5AYL5; C8V152;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=COPII coat assembly protein sec16;
DE   AltName: Full=Protein transport protein sec16;
GN   Name=sec16; ORFNames=AN6615;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000110; EAA58144.1; -; Genomic_DNA.
DR   EMBL; BN001301; CBF71102.1; -; Genomic_DNA.
DR   RefSeq; XP_664219.1; XM_659127.1.
DR   AlphaFoldDB; Q5AYL5; -.
DR   STRING; 162425.CADANIAP00007395; -.
DR   EnsemblFungi; CBF71102; CBF71102; ANIA_06615.
DR   EnsemblFungi; EAA58144; EAA58144; AN6615.2.
DR   GeneID; 2870538; -.
DR   KEGG; ani:AN6615.2; -.
DR   eggNOG; KOG1913; Eukaryota.
DR   HOGENOM; CLU_001147_0_0_1; -.
DR   InParanoid; Q5AYL5; -.
DR   OMA; LERWKGA; -.
DR   OrthoDB; 56582at2759; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; 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   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..1947
FT                   /note="COPII coat assembly protein sec16"
FT                   /id="PRO_0000295537"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1462..1760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1773..1904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..634
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..769
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..907
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1481..1497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1627..1641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1674..1726
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1818..1838
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1853..1882
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1947 AA;  207506 MW;  6519256F78BF8323 CRC64;
     MENSNSEASA VWNPALRTDD NHETAATVEE ISAPVSSDVA PLTPKATTAN TDIVPDAIDS
     INTESPAREE TAELPLNEHT HTVPGAAEPV NVGSAGFIET AEAPPTAIDD PGAVPVAVSP
     NGETSAPAIA TDVTSVSENT VPDVTESSSV EPTALIEIAQ AESATGEDFN QAETREEFRE
     EAAELFSAAA DENQETDAFK PQAELAAAPG DGYNNLQSMQ EEHVQEGQTH QLEIDTSVNA
     AQGSSDYPTP GWVYQQGIAD HATPIDGELR STNHDLWGSP KSVDNGEDRF FDQLRTQTKP
     IYFPSEESRF EEGVPLLDGS AEAPVEAAPV EATPVEQAVP QPGQLDRVFE GDEDEDDGFF
     SSAQQPATEN EPQEPVHIQR KSTSQVLDSL NTNRDGVHSP LSPTAEEFND IIAAAASKSP
     ENVQEPASEE DLAARWQAEL SDDDLEVAPV EEDLAAKWQA ELDDDDLLLE DEPSDLAQNT
     AAEVVNGHGV EPNLQALGSP FGTPQNPSKP KPAQSVYTPH QPSTADLVQS VPIPGATPLS
     SSAPYSTSYF QPRPEPPAPA VRAESFAERP KEGYKSPYDL PEDLAPRRKP ATKPVVSSAA
     NVPAPPPRSS SFTAPPPPQS SSGVPVPPIN AATLPPASKP NAPVASAPKN FYEELPLPPV
     RPRSRPAESG RYTPKFNTAS PAFVQPPPAA HPVTNPYAQL SGDTPQSQLQ QPEKLGPYAN
     NVGSSSQSAP AVPPINSRYS PKPPTLQPGV KPPASPRYSP APPPPAAASA PLQRYTSQPS
     VIPGQTVTLP FQPRTSSPLA HHEKVSYQPN EASRKPSFPQ PTSPVTGQPS HTETAAPMSP
     RSSQVQASGP SAVDTSSSYQ QTSPPRNPYA PPSYLEEFSR RVSHVNNSTP SAYTPPPETP
     PFVPPRRSQT QSPTQQQSGP RLSVPSVDPL KRPASVHAPS SPTKTSHTYA PMQPSSHIRT
     ISQSLEFIPP SDGQELDPLQ RWKGAPIFKF GFGGTVLSSF PKHVPRYSAG QTAPKIKPMP
     GDVKTTQLKD VISFPETIVR HPGPLRNKSK KKDLVAWLSS RIAAFENEGV PQNLQAYPDS
     YKRRDEKILL WKAVRVLVEH DGGMQSTPDL QEALRGILFP HLQTNGLEPM YSDSLQSFGA
     EVINASSLSD SAESKPLSSI RNNLLIGERE KAVWSAADNR LWGHAMIIAS TLDKSIWKQV
     VQEFVRREVR SNSGNPESLA ALYEIFAGNF EESVDELVPP SARAGLQMVS KVDGHGPSKD
     ALAGLESWKD TLGLVLSNRS PEDHRALLAL GRLLLSYGRI EAAHICLIFS RAAVFGGPDD
     PQASIVLLGV DHVHSSPTAL LDDDAILLTE AYEYATSVLG ASPTSTLPHL LALKLVHAWS
     LTDQGRKSEA QQYCDAITAA LKATTKQSGY HHQHLFFGVD ELSARLKQTT GDGGSWISKP
     SMEKVSSSMW NKFSNFVAGD DSDAASTGSG KGGETGFGPF AQISGTPTVS RSPSVTDLYG
     QYPMPVAQQV PGAGTSRYQP NNQNAPNSSP DQGRGRSSLD SQRSASFGLS YGQRRGSQEY
     GHPSESPMYG GGPFYGSPTA GYQSTPPQTS YMPLAPVEED MAQQAYTPPT ATPQGLFGHD
     LPYQPPAQNP FDQSTGPEAP ASQHTEADGY MPPTGNTGYE PPASNTLEVE VTEESEDEKP
     RKKLTMDDED DDDIAARAEA LKKAEKARKD READEAFRKA AEADAKKPAP AKSSWWGWIK
     GGNKEEANSG KPIRAKLGEE SSFYYDKELK KWVNKKDPNS ATPARATPPP PKAMGPPSRA
     ASGSSMPPSG TAGLGSRPPS VAPPPSGSPA PSSLGLPPTP GLGPARSAST GAVPPAGNAS
     SRPGSSAGPP PRPSTSLSHA SSIDDLLGAP QARKGATSRG RKKGRIRDLP HLAYRSVYPC
     IANYQPPYIV VNLHAISSGS MAWLLVL