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Database: UniProt
Entry: A0A179A118_9EURO
LinkDB: A0A179A118_9EURO
Original site: A0A179A118_9EURO 
ID   A0A179A118_9EURO        Unreviewed;       996 AA.
AC   A0A179A118;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Protein transporter SEC24 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AYL99_01659 {ECO:0000313|EMBL:OAP65687.1};
OS   Fonsecaea erecta.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP65687.1, ECO:0000313|Proteomes:UP000078343};
RN   [1] {ECO:0000313|EMBL:OAP65687.1, ECO:0000313|Proteomes:UP000078343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP65687.1,
RC   ECO:0000313|Proteomes:UP000078343};
RA   Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA   Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA   Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA   Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA   Attili D.S., Gorbushina A.;
RT   "Draft genome of Fonsecaea erecta CBS 125763.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025471}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}. 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 SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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:OAP65687.1}.
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DR   EMBL; LVYI01000001; OAP65687.1; -; Genomic_DNA.
DR   RefSeq; XP_018699054.1; XM_018833175.1.
DR   AlphaFoldDB; A0A179A118; -.
DR   STRING; 1367422.A0A179A118; -.
DR   GeneID; 30005829; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000078343; Unassembled WGS sequence.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR   Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR012990; Sec23_24_beta_S.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR   PANTHER; PTHR13803:SF4; SECRETORY 24CD, ISOFORM C; 1.
DR   Pfam; PF00626; Gelsolin; 1.
DR   Pfam; PF08033; Sec23_BS; 1.
DR   Pfam; PF04815; Sec23_helical; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   Pfam; PF04810; zf-Sec23_Sec24; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR   SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078343};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          280..318
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          356..604
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          611..695
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          707..806
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          835..908
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  108713 MW;  E1FAFF35907E1EC1 CRC64;
     MASYGSQYGS GQGQSYQMNQ DPRYADPQMQ QHPPSFPPSV SPQPAYPQYG VDPNAQHVYA
     NAQQASYLGQ PEGHVPQQQD AMNGMNRLAE KMSGLDMAAA PARSHRKKER HAYHDIGSAS
     ATAPAGGAVP AGPFGQPQFP AVGSQGAPGA MAGQPAENAL INSTDKLRMG EEAVATQGRV
     NPEQIPSVAR SRDVATQYYQ LNVYPTMEKH LPPPAAIPFV AHDQGNSSPK FARLTVNNIP
     STAEALASTG LPLGLVLQPF APLQEGEQPI PVLDFGELGP PRCRRCRTYI NPFMTFRSGG
     NKLVCNMCSF PNDVAPEYFA PTDAAGVRLD RLQRPELMMG TVEFLVPKEY YTKEPIPMRW
     LFMIDITQEA INRGLLHTVC QGILDALYGR DGEVPSDEGS TFVGLPAGAK IGIVTYDKEV
     QFYNLAPGLE TAQMMVVTDL EDPFVPLADG LFVDPQESKD VITALLKAIP TMFSAIKHPE
     PALLPALNAA LAAMTATGGK IICSLSTLPT WGPGRLHLRD DGKGRDTDAE RRLFTTEHPG
     WKKTAGAMVT AGIGVDFFLA AAGGGYMDIA TIGHMSRLTG GEMFFYPNFV APRDSLKLRL
     EIQHSLRRET GYQALMKVRC SNGLQVSAYY GSFLQHTFGA DLEIGTVDAD KAIGVTFSYD
     GKLDAKLDAH FQAALLYTSA TGQRRVRCIN VVAAVNEGAA DTMRTVDQDA VVNIIAKESS
     SKISEKSLKD IRAHITEKTI DILAGYRKNF SGSHPPGQLV LPEHLKEFAI YTLGLIKTRA
     FKGGVEPTDR RVHSARLMRS SGVTETALYL YPRIYALHNL SPEDCFANAE TMQLVVPPTL
     RASFARVEEG GVYLVDDGQI VLIWLHAQVS PNLLEDLFGE GKTSLQDLDP MMNELPVLET
     HLNAQVRNLL QYMSTVRGSK AASFTLARQG LDGSEFEYAR MLVEDRNNEA QSYVDWLVHV
     HRAIQMELSG QRKKEDTGDH EGILSNLTSL KAPYWT
//
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