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Database: UniProt
Entry: A0A1L9UC37_ASPBC
LinkDB: A0A1L9UC37_ASPBC
Original site: A0A1L9UC37_ASPBC 
ID   A0A1L9UC37_ASPBC        Unreviewed;      1909 AA.
AC   A0A1L9UC37;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN   ORFNames=ASPBRDRAFT_198669 {ECO:0000313|EMBL:OJJ69103.1};
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ69103.1, ECO:0000313|Proteomes:UP000184499};
RN   [1] {ECO:0000313|Proteomes:UP000184499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC   {ECO:0000313|Proteomes:UP000184499};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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. {ECO:0000256|ARBA:ARBA00024687,
CC       ECO:0000256|RuleBase:RU364101}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the SEC16 family.
CC       {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR   EMBL; KV878689; OJJ69103.1; -; Genomic_DNA.
DR   STRING; 767769.A0A1L9UC37; -.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_198669; -.
DR   OMA; YKSPYDL; -.
DR   OrthoDB; 1361743at2759; -.
DR   Proteomes; UP000184499; 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   CDD; cd09233; ACE1-Sec16-like; 1.
DR   Gene3D; 1.25.40.1030; -; 1.
DR   InterPro; IPR024298; ACE1_Sec16_Sec31.
DR   InterPro; IPR024880; Sec16.
DR   InterPro; IPR024340; Sec16_CCD.
DR   InterPro; IPR024468; Sec16_N.
DR   PANTHER; PTHR13402; RGPR-RELATED; 1.
DR   PANTHER; PTHR13402:SF6; SECRETORY 16, ISOFORM I; 1.
DR   Pfam; PF12932; Sec16; 1.
DR   Pfam; PF12931; Sec16_C; 1.
DR   Pfam; PF12935; Sec16_N; 2.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|RuleBase:RU364101};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU364101};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU364101}; Membrane {ECO:0000256|RuleBase:RU364101};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU364101};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364101}.
FT   DOMAIN          195..348
FT                   /note="Sec16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12935"
FT   DOMAIN          380..510
FT                   /note="Sec16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12935"
FT   DOMAIN          979..1096
FT                   /note="Sec16 central conserved"
FT                   /evidence="ECO:0000259|Pfam:PF12932"
FT   DOMAIN          1155..1456
FT                   /note="Ancestral coatomer element 1 Sec16/Sec31"
FT                   /evidence="ECO:0000259|Pfam:PF12931"
FT   REGION          1..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1130..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1480..1757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1770..1909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..580
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..615
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..680
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..764
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1604..1635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1670..1722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1806..1842
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1843..1859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1909 AA;  202523 MW;  8B68AE99BBCCE4E8 CRC64;
     MAQSDVAAVW NPAFRSDNNA TPVPTGPASL EIDTSIEATT IPLGSPMETP HEYSISDIAF
     PDPDTAAPSQ EAASPDMIDT QSSPKPDQIP TRDGVPEASS GDVEAIPEIS DDHETPSLEE
     PQLGPAHDSK DVSLDDPEGQ ITETQPVQPQ AEEPVPTEAP AAQGMDVEEQ SSTSDASEQD
     ATEPADTNGE TQSSHDIWGR PANEDAAEDD FFNQLKTQTK PIYVPPENES RFEEGVPLLD
     DSAESPVKPT ATEESQIDNF FAGDDDDDDD DGFFKAVQNS PPPNESQPAS HITRKSTFQV
     MNSLGVSLDS PMSDAAPAAQ EFDKALAAAA TDNSIEKPSL EEDSAAQEFD NVLATAATDN
     GIEKPSLEED PDAQEFDNIL ATAATNSAEN PSFEEDPAAQ EFDNVLAAAA TDNGIKKSSS
     DEDLAARWQA ELAEEETEAA PSEDDLAARW QAALDDDDLL LEDDIGGAVA EQAPTSNEAT
     SNAAVPGLSS PFGTPQTSVR PSAPATAYTP HQPSTSDLLQ GIPVPGAAPS ANMATTADYF
     TQPPRPNVTA SKAESFAERA KEGYRSPYDL PDDLTRPRRP VASHKPVVTQ PGITPPPQRS
     NSIPVPPPST SMPPPLGAQP NAALSTAKVA APKNFYEELP LPPPRPQSRP ASSGRYTPGA
     NAMQPASSHP PPPPANPYAS LPTASPAAAD AYPQPQVQQP ERLDPYASLS APGAPSGPAP
     PSATSRYSPK PPTLQAGIKP SPSPRYSPAP PPATAPPPRN RYASQPSAPP SQGVALPFQP
     RTSSPLAHHE KVSYRPQEHL EKQPPSMEQP AIIPPIEVQS QPTGPVEYSP IQPSEATHAP
     EAANMGTSVH QMSQQPMSPP RNQYAPPDYV DGFSKRIAPI ANAPPVPVLP TDDPTFVPPR
     RSLTQSPSQQ TLGPRLSVPS VDTLQRPASV HGAGSPTKAV NPYAPAQMSA HNRVASQSLD
     FIPPTDDQQF DPLERWKGAP IVQFGFGGSV LSCFPKHIPR YSAGQATPKI KSTPGEVKTH
     QLSDWIPVPD TIARHPGPLK SKSKKKDLLA WLSSKIAAFE NEGVPESVYM HADSQKRSEE
     KILLWKVVRV LVEYDGVLEG SPEIQKSLRQ IIFPHLQDVD SAQPYGNGLP SFSATQSLDA
     PSRPDAADPQ AVESIRSNLL VGEREKAVWG AVDHRLWGHA MIIASTMDKS VWKQVVQEFV
     RREVRSASGN TESLAALYEI FAGNVEESVD ELVPPSARAG LQMISKVDGH GTSKNALDGL
     DSWRDTLGLV LSNRSSEDYQ AILALGRLLQ SYGRIEAAHI CFIFSRAAVF GGVDDPQASV
     VLLGADHQHL SLAALHDEDS ILLTEAYEYA TSVLSATPKP TLPHLLAFKL VYAWSLADQG
     RKSEAQQYCD AIAATLKATT KPSPYHHQHL YFGVDELSAR LRQTTSEGGS SWISRPSMEK
     VSGSMWAKFN SFVAGEDNEA GSAGSAKAGD GDIGPFAKIA GTPTVSRSPS VSDIYGTYSA
     QPNYSSGPSR YQPNNQYAPT SSPEQLRGRS SLDSQRSSSF GFGFGQRRGS QEPSTPIESN
     MYQGGMLYNS PPAVGYQSTP PQSSYMPLAP VKEDLAPQHH AEASAGSVGQ SYGSGSPYQP
     AGYGSFDQSF MNQAAPSDGA GYMPPGVSSG YEPLATESHL EPAAAAPEEA NEEEPPKKKS
     FMDDDDDDDI AARAAAIQKA EKARKDREAD EAFRKAAEAD AQKPAPAKKS WFGGWFAGGK
     KEEQNLNKPI RAKLGEENSF YYDKDLKKWV NKKDPNSATA ARATPPPPRA SGPPSRTASG
     SSAAPPPPAS ASPMMPPPSS RPPSTTGMPP PPGSPAPSSL GVPPPSIQRS VSTGAAVSTP
     PSGLAAPPRP ATSLSNASSI DDLLGAPTAR KGAAAKGKKK GRYVDVMAK
//
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