ID A0A1E4SY06_9ASCO Unreviewed; 2679 AA.
AC A0A1E4SY06;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=CANARDRAFT_8727 {ECO:0000313|EMBL:ODV84373.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV84373.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR EMBL; KV453857; ODV84373.1; -; Genomic_DNA.
DR STRING; 983967.A0A1E4SY06; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000094801; 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; 1.20.58.940; -; 1.
DR Gene3D; 6.20.50.30; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
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.
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:UP000094801};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1282..1360
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1427..1692
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1972..2046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2118..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2204..2261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2289..2319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2377..2561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2576..2679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1040
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1972..2018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2132..2156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2157..2171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2210..2256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2289..2311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2377..2409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2443..2467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2475..2491
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2492..2530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2539..2561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2605..2627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2679 AA; 292323 MW; 8849AE7210CF14C3 CRC64;
MGKNNKSKSK ANKKAKGRNA TNNNNNKAII PETSSNDSVS ASHESISVTA GDAGDAVDNS
EEQVAEKDDD ALPVISTSKA DDSLSQDDFN GLEQVISKPK SFLVDVLQQT TSEIDKVESL
NIVPDQQESN SADSYSNEFQ EVTNVFPVEC SSKSTVVDGL HTESSQDNCS RSSLRSDKEI
NGGYVQGHGS KEVLEHGQDQ NNSEVLDLEQ DQESVLLSPK HEHILQSPSF NDNDLLPWDE
KAPENYNGTH QDDAKLMPWE ASQSTEINSS LAEDSANATM SHVGDEYQQH EQIDSQEHQQ
SQLGSNFDTS STLPNSSSIL EAFQVNETNS SHGVHDEDTE QNNIPWMEHS NQVENGKMPW
EESSTIDSQK LEPSQSEEPW NQHQVHSEVI PWEEHTELQK PDTNIKNQIE QPATILKNSP
TSAHEESVEA KVDVMPVEET NSQREKEEDL PKELVFNPQE DVMPWEETIT AHKEDIPFEQ
LSFGHQEEVM PWEESITAHK EDIPFEKLSF GHQEEVMPWE ESNADQKEEV LPWEESNVVH
EEKDTRSKEL SFNHQEEVMP WEESNVDQKL DDVPPEQSNV NHQEEAMPWE QSNVEHQQPV
ATGEQSGNLD KPYSLENTTD SLDIASTTVV YSPTKHQTME LSMPDSQQGD HDDSVLSVVD
PTTIQNVDEE TTNEISNNVE IDDDKLRFLE MDDDLLLEDV MDDDFLEDDL PEQAVDTVIP
TYAPAELLQP VSEQPATNRY KPSAPPTSRY QPATPQARFP QMQPPLQHQL QPSNNHSGLY
GFPDSNQRQS FIPSATNPLA NLPPQIHANL QNKELQQKLE KEKKKSDAYD FPSDILAKHQ
PKPKAAPLTN IYTVVESRKQ QQQQQQQQQG SVPVALPPPP PISGEPGFGA PPRTGSAMSL
SSNPANSVAR TLKPKKSFFE ELPLPKIPMK SSLHLKNPYE AIENSMHHQN QQQPVRSRAS
TLKNSDAGSP LVAGNTPLNP YAPPAINNMS TINKANPYAP HLAGTKSSPY SPANISTSQP
SSGAPPVFTP SLPTPQARKP NNPYAPSEIG GHARTASLTL TPAPVNPSVV PVPHMSPMKQ
IISPVPQGNQ FASQGLGVQG QLNMKVKPAD QGPYGDPGSA STGISSSSSA GISPNLSRVQ
PANRYSPYAP VQQQQQQQQQ QQQHPYGKPV ATFPPAQNKY ASQPLDSVYG DSAKPDITSP
IVSGSSRRGH FLPPHRDTAV TGSNSVALAG GSSSAKKLPP YNVPPASAPA PVVINPENLV
RRQWPLFSFS ASSKASALIP TTDAYGHQKF NIKIVDISSV LMPDRQVQTF PGPLIKNKSK
RKDLDKWLGD KLGFITEDIN GPYITGEQLL FAVLKVMVNH IQKQGDFTTS KVYIEAVIQV
LNPSLNLESL NSDDSVDFSG LSHYLQQFGS TKPFNAYKVD SAGLINIYTL LEGGNSKGAL
SFAIQEHDWA MAFMIANIMG SDTVAEIVKL YAQTLLNHND LLVQNLSFYF QSSSDKGFKS
ELYLGKEKWL VENFKSVIPF LLLNNKSPAN ILIQLGNLLA GAGFKYYAKI CHVLSGMPLI
PKNNSELPND IYGMIVEEIY EYVLLSSSNV PPALANGFPH LLPIKVKHAG YCADCGLSSD
ARRYCDYVGT ALKSKLLFVD PATSISHAQL LQRLAQVETE TSGWFGGKLA RPNLDKVWGQ
LDKSFSKFVA GEELIDKSKP AAEGVFSKFS PSVSRNASQL DLSSLQPQSQ PIMSGYQSST
NISTMGNPYG SVSSSHSHSA PTTSSNSTVV QGGSALNPYT PYSQSKPSHS QPQQNRLNAY
APPSAAVHNQ VHLQGFGSPS TKSSNFSDSA LVPTTPSFNR TSTGHSYQQN ENSSNVYSAY
QPPATLQHKA SRENISQPPP MPHSLSRNVS YTQSQGGLGD HSPSTSSVFP AKASYSPYAP
PPKLATQQGP PTSSLTPYNG ATQNLVKSSA PVLPDVNPAF QEVPLPLAET LAQQQHETHQ
PSFQNPPHSM QSVTPSQLAP LNHSSPLHNG QQSDDVPVFN PSAAPKKPSK YGPLNGAQAR
PVASSTDSLL EKLDSMSLIK ENHAPSISSI KTDVKMKEPT AYKPFANSYA HIEVSPTLDS
ESLGNHEVEE DEIPSILKDI APEDKEDTEE TEKLEVESTD HIQDSTETDS EHITEVDGET
NSLTTAASEA KLDEQIISEV DNGEEQKDVD SEAEAVETVV SAVETDVSAV EAPPTSSPDS
ETLPGRRSSE TTVTDTPYDP YSSISLAASR SNGPPLANPY SAAMASKKPT AISKKVNPYA
AVIDAAVKSR APTTSNNPYA PRKTSTAGAP PPISSPYAPS AHKKVSVAIG NRYAPVGETA
ALSSPKEEEQ QVEEALIPDE SMYSYFGYNT SQVPEVEETV EHNDAETELD GVHSKTEEPV
YKEPDFNVVD DEPLPPPSDN IFNPSAAMGG ANHLRKMFNP PSAEVSDMTS KPPATRKSPT
IVTNDSRRYV AEDNDDEYYD DVIDDDEDDE SEIQKQKEKE IMKERERIAA ERKKKEEDDA
KAKTQQQEAS AAKKKGDGWL GWLSKKKDDG VKPIKAKLGE ENSFYYDEKL QRWVNKNASP
EEEAAAAPPP PPMKRAAPVT PGQSNSGSPA PPSPVGSAPP PRNGMGMPPR APSSLRGASP
AMSARKADNI DELLSISAGT THKSKRGPRR GYVDVMSKK
//