ID A0A0A2L2P9_PENIT Unreviewed; 2004 AA.
AC A0A0A2L2P9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=PITC_031300 {ECO:0000313|EMBL:KGO74279.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO74279.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO74279.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO74279.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO74279.1}.
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DR EMBL; JQGA01000665; KGO74279.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2L2P9; -.
DR HOGENOM; CLU_001147_0_0_1; -.
DR OMA; YKSPYDL; -.
DR OrthoDB; 1361743at2759; -.
DR PhylomeDB; A0A0A2L2P9; -.
DR Proteomes; UP000030104; 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:UP000030104};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 374..623
FT /note="Sec16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12935"
FT DOMAIN 1077..1194
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1254..1552
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1901..1915
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1916..1941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2004 AA; 214040 MW; E71D51E91B28A1A4 CRC64;
MAHQATDNDS ESWNPASRPE NNNSSATMSS IQGGLSDPIA ANKPKDGSLD DIVSPRSEDF
SAWDMSEEVD AIQPQYTSLD VLVNNASPVV DQPVCLETDS VDKKSQNSIE DFHTTIAPSI
ENADTALSPT LPEPRPAQPV QTEAPSVQPG VEASNSSFTT IDGPVDVQTE RLDTAVPTVA
PEQETTESTF VRDTTPREEQ TIAPEPTLDT LEHQNTTHST PTEELFPRTD DGNTDSENPW
TTFEKDLSNT LPSTEEATPL RKTSHTIPEF ASTSTQIQDA DEPKFVEEVV RPSPEETAST
GATFDEESTD IFNSTEKAIA PTENEEVDDV SRSIIVGSEN TDSPAPIMEA FIPTNEAHPV
SAAADVDTAN QDQPFWTSEP SGEVDCDEDD FFNQLNSQTK PIFAPPEAES RFEEGVPLLD
ESTPASPQRS LVEDKSIENV FSEDDDDDAD GFFSSAPKLE DKNGDEDFFG STSKEEAEEQ
PVVHLALKST SLVLESAGFA LDSPVSDASA AAQFDDALKA ASMEPQTTAD PSEEELAARW
EAELADSLDD ALDDDLAARW EAALDDDDIL LETETAQSVS AQENIDQTPI RPTHNGLSAD
LNSPFQTPQA FSQPRPVPNI YTPHQPSTGD LLQGVPLPGT APPATGPMSS YFSQPPQNPV
AIRGESFAER SKQGYKSPYD LPDDISRPRK PVAAYKPVPA TVTSMPPPPH LGVSGIPIPA
AAGFPTTAAP PSSVSAPPAP KSFFEELPVG PPRSRPASSG RYTPNPQAAP AMTGSSLPPP
QVQYAPAAPP APQHVALPIQ STLQPPEQLD LYASLASSAP AGPPAIARYS PQPPGSQVPP
KPPSLPRYSP APPPTSSVRS RYASQPLNVP GQNLPFQPRT SSPLAHHEKV SYQPDHLHKP
PYLEPAINLS PPRGQRAGFG QIPPSGPPYH NGPASPPRRE SAGSPVQPSP PQSRYAPQEY
LNEFAQRLAP APEHAPPAPV TNVYMSPPPS DIQMGPLRRS QTQSPARDLT SPRSYGQNID
AIQRPASVQV SGSPTKTVNP YASVQAASQN RAPTQHLEFI VPNDGQEHDP LERWKGAPIF
KFGFGGSIAS CFPKHIPRYS AGQAAPMIQP TLGEPKISQL SEWLPSADNI VQHPGPLKAK
AKKKDLVTWL SSKIATFENL NLPTYEQVQS DTRKRQEEKT LLWKVVKLLV ENDGNLDSSL
EIQKSLRQII FPNLPIPDAD GSYTSSLAAS GGFAPSELPS QPDAVDAQWL EELRLHLICG
DREKAVWSAV DRRLWGHAMI ISSTMDRSIS KQVAQEFVRR EVRSKSANTE SLAALYEIFA
GNIEESIDEL VPPSARAGLQ LISKADGQGS TKNALEGLDK WRDTLGLVLS NRSSEDHQAL
FSLGHLLTSY GRTEAAHICY IFSRAAVFGG PDDPKANITL LGADHQRCPS SLMDEDAILL
TEAYEYATSV LSNSPTAQLP HLLAFKVLNA RCLVDHGRNL EAQGYCDAVA AALKATTRPS
PYYHQHLFAE VEELSARLRQ TTSDSGSWIS RPSMEKVSGS MWARFNSFVV GDDSDAASTG
SGKGGPPTIS RSPSVSDIYG SYPGAAAGVQ PIPTSGPSKY HPSSQYAPNA SPEQFKGRSS
MDSQRSASYF PPVGQRRSSQ ELSPSIDQQI SYGAPVYGSP NAGGYQATPP QSSYVPLAPV
EEAMSPTEAP SAAQPVVNGL FYQPPGQAAT STESPYYQGP PGMPAGIPDS ESPYAPPVAS
SSYEPVSYEP VSAGVDMGYV AQEDDPSSTV EQPKKQSIMD DDDDDLAARA AAIQKAENDR
KANEAFAKAA EEDAKKDAQQ SGKKGWFGGW FGGAKKEENN SGGGPIRAKL GEKSSFYYDK
DLKKWVNKKD PGSSAPVHAT PPPPRGSAPP SRTASSGSMP PKGAPPMPPM PPMSVSSSLP
QSSSTAAPPS LSSSPGFSGL APRSASTGAA MPTPPGSSSG PPPRPSSSLT HASSIDDLIG
APQARKGNAV RGKKKGRYVD VMAQ
//
