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
//