SEC13_KOMPG
ID SEC13_KOMPG Reviewed; 289 AA.
AC P53024; C4QV39;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Protein transport protein SEC13;
GN Name=SEC13; OrderedLocusNames=PAS_chr1-3_0057;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10923020;
RX DOI=10.1002/1097-0061(200008)16:11<979::aid-yea594>3.0.co;2-c;
RA Payne W.E., Kaiser C.A., Bevis B.J., Soderholm J., Fu D., Sears I.B.,
RA Glick B.S.;
RT "Isolation of Pichia pastoris genes involved in ER-to-Golgi transport.";
RL Yeast 16:979-993(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=10189369; DOI=10.1083/jcb.145.1.69;
RA Rossanese O.W., Soderholm J., Bevis B.J., Sears I.B., O'Connor J.,
RA Williamson E.K., Glick B.S.;
RT "Golgi structure correlates with transitional endoplasmic reticulum
RT organization in Pichia pastoris and Saccharomyces cerevisiae.";
RL J. Cell Biol. 145:69-81(1999).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. It also functions as a component of the
CC nuclear pore complex (NPC). NPC components, collectively referred to as
CC nucleoporins (NUPs), can play the role of both NPC structural
CC components and of docking or interaction partners for transiently
CC associated nuclear transport factors. SEC13 is required for efficient
CC mRNA export from the nucleus to the cytoplasm and for correct nuclear
CC pore biogenesis and distribution (By similarity).
CC {ECO:0000250|UniProtKB:Q04491}.
CC -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Component
CC of the nuclear pore complex (NPC). NPC constitutes the exclusive means
CC of nucleocytoplasmic transport. NPCs allow the passive diffusion of
CC ions and small molecules and the active, nuclear transport receptor-
CC mediated bidirectional transport of macromolecules such as proteins,
CC RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the
CC nuclear envelope. Due to its 8-fold rotational symmetry, all subunits
CC are present with 8 copies or multiples thereof.
CC {ECO:0000250|UniProtKB:Q04491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q04491}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; U52430; AAB01155.2; -; Genomic_DNA.
DR EMBL; FN392319; CAY67109.1; -; Genomic_DNA.
DR PIR; T10477; T10477.
DR RefSeq; XP_002489393.1; XM_002489348.1.
DR PDB; 4L9O; X-ray; 1.60 A; A/B=2-289.
DR PDBsum; 4L9O; -.
DR AlphaFoldDB; P53024; -.
DR SMR; P53024; -.
DR IntAct; P53024; 5.
DR MINT; P53024; -.
DR STRING; 644223.P53024; -.
DR EnsemblFungi; CAY67109; CAY67109; PAS_chr1-3_0057.
DR GeneID; 8197368; -.
DR KEGG; ppa:PAS_chr1-3_0057; -.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; P53024; -.
DR OMA; TVDTGHE; -.
DR Proteomes; UP000000314; Chromosome 1.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061700; C:GATOR2 complex; IEA:EnsemblFungi.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037596; Sec13.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Repeat; Translocation;
KW Transport; WD repeat.
FT CHAIN 1..289
FT /note="Protein transport protein SEC13"
FT /id="PRO_0000051205"
FT REPEAT 7..37
FT /note="WD 1"
FT REPEAT 51..83
FT /note="WD 2"
FT REPEAT 97..131
FT /note="WD 3"
FT REPEAT 147..178
FT /note="WD 4"
FT REPEAT 197..227
FT /note="WD 5"
FT REPEAT 244..274
FT /note="WD 6"
FT CONFLICT 148
FT /note="V -> G (in Ref. 1; AAB01155)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="W -> S (in Ref. 1; AAB01155)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4L9O"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4L9O"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:4L9O"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:4L9O"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:4L9O"
SQ SEQUENCE 289 AA; 32105 MW; C711A2810ED1F049 CRC64;
MVTIGNAHDD LIHDAVLDYY GRRLATCSSD KTIKIFEIDG ENQRLVETLI GHEGPVWQVA
WAHPKFGVIL ASCSYDGKVL IWKEDNGVWN KVAEHSVHQA SVNSVSWAPH EYGPVLLCAS
SDGKISIVEF KDGGALEPIV IQGHAIGVNA ASWAPISLPD NTRRFVSGGC DNLVKIWRYD
DAAKTFIEEE AFQGHSDWVR DVAWSPSRLS KSYIATASQD RTVLIWTKDG KSNKWEKQPL
TKEKFPDVCW RASWSLSGNV LAISGGDNKV TLWKENIQGK WESAGEVDQ
