ID F2SFP0_TRIRC Unreviewed; 1789 AA.
AC F2SFP0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=TERG_01228 {ECO:0000313|EMBL:EGD84955.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD84955.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; GG700648; EGD84955.1; -; Genomic_DNA.
DR RefSeq; XP_003239246.1; XM_003239198.1.
DR STRING; 559305.F2SFP0; -.
DR GeneID; 10374151; -.
DR VEuPathDB; FungiDB:TERG_01228; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_001147_0_0_1; -.
DR InParanoid; F2SFP0; -.
DR OMA; YKSPYDL; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000008864; 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; 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:UP000008864};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 232..459
FT /note="Sec16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12935"
FT DOMAIN 854..971
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1021..1325
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..772
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1789 AA; 191448 MW; DBC67B28918511B5 CRC64;
MSDDSSSKPS AEPEVAAALP DSQECSAPTE TIPSRPPTDS DPSDDHQPSE SQEVSQDTET
STSLDQPTGV PGLGDTAADA ENSELLTLLE SSTETPQQDK LEAPSVRVDD TEDVSQPTNI
QASQPNVPEV TLTEDIISAG HSDSIQPITQ SSDEQPSLLS RSNTTKLLAR DDIVSRTNSF
PTVNSTNEPD HPTTSAPQVF DSAESQHDSN NDTPNVPSTE SDVNSGSTHA APLWNDDVDN
EAEGEDFFNQ VSTQTKPIYI PPEFAESRFE EGLPLVDNGD QSNDQQAAQP KQQSALDSVF
SEDITTDEAG FFSSDMSHAA EPSEAPPTLH RKQTSQVLDS LRMDDAFRGD ESPIEPPGAP
CEQLSTSEAV GGHQTSKDDA TTMENLDENE LAERWKAALD DDLLDDELLD DDLLDNDNAA
QQEDEKPPAP PPSQRYAPNT STCLPQSRPA PPPINPYAPH QPSSSSIMEG IAPALYGEHA
QPISPVSASA ESFSNQPKAG YKSPYDLPDD LQPKRRIAPR SASNISQPYQ PIPDSRPSSS
YSAAPLQTAP PVAPTNPYAP QPQPQSQKPA APNNFFEELP IAPRSRPSTR GRYAPPPAEA
GRQAPAGPQM MTPTSQQHNE PQPQGQYGLQ APPRMDPYAN IIAPAGPVAT KPATQYSSRP
IGKPAASGRY SPAPPLSSSA PSHSYMPNHA GITLPFQPRT SSPLAQHDSS HVRPRVHPES
PREGSLGSQE SAQHLSPPTA HNDFGQRNYA PMSNVISSPP SSMPPPSAPI RMSPPRRSQT
QSPGKRIYSQ GHPSIIQDNA QRPASAHAPS GPAPASHFPL ARAMTVDSHP APAVDFIAPA
DSHSLDPLER WKGAPIIKFG FGGSLITSFP KRVPLYSTGQ LTPRMKPVPG EIKLRSFNEA
IPESVMPAKF PGPLKSKSKK KEVITWLSNM ISSFEHEDPQ GLVSLTQGEF QAKVEKIMLW
KVLRTLVEHD GVLRGAPDAE KSLLSILSPI TPQNEQGAST IGSTNALYGK EEPANVSLDA
IQHNLLLGER ERAIWDAVDH RLWGHAMLLS STLNPSVWKQ VVQEFIRREV RSVGENTQSL
AALYEVLAGN FEESADELVP LSARAGLQLV NTRTGQGPTG NALDGLNKWQ ETLSLILSNS
SAQDDQAILA LGRLLSSYGR VEAAHICFLI ARSNTNPIFG SLQDSNAYIV LIGADHKRYP
FTFMADSTAC LLTEVYEFAT SVLTATPLHV LPHLQAFKLQ HAMTLAETGH RSEAQQYCEA
IGALLKTATK LSPHYNQQFF IELEELSNRL RQSPGDSASS WMSKPSMEKV SGSMWAKFNS
FVAGDDSSPD SSDPSKPHED QGPFANVVGT PPVGHSPGGP ESFGSYFPTH QQQPVAIPAS
NSRYAPNNQY APFSSPDQLR GRRSLDSQRS PSRGAAARSY SQRRHSQDPS TGYENSYAPL
AAGNPYSPSP VAPQPTTHST PLPAHSPLAP VEEASSSLAP STTSEQAPGM GVSAPGPSSF
QPAYQQVNAT YSPPTQESQG GYEPPSEGGY QPPSYEPPSY EPPMNEPESP GSEEAEEKKP
KPRKSFMDDD DDSYTGKGAV AAAPTNGVET DRGRRDREAA ELVRKAAEED AKRPPPDAKK
GWFTGWFGKR DPSASGGPIR AKLGEQSSFY FDEDLKRWVN KKDPNSATSS TSALPPPPKG
SASGSRSASA EQRPPTSASV ASAPDAVPIP LAKQLSAQGG PNSPYGSAAP PSSLGVPGGT
PPLTPSSRPG TALSHASSID DLLSAPTSKK GGTLKGRKKG RYVDVMAKS
//
