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Database: UniProt
Entry: M4B3M5_HYAAE
LinkDB: M4B3M5_HYAAE
Original site: M4B3M5_HYAAE 
ID   M4B3M5_HYAAE            Unreviewed;      1001 AA.
AC   M4B3M5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP800874, ECO:0000313|Proteomes:UP000011713};
RN   [1] {ECO:0000313|Proteomes:UP000011713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA   Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA   Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA   Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA   Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA   Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA   Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA   Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT   arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [2] {ECO:0000313|EnsemblProtists:HpaP800874}
RP   IDENTIFICATION.
RC   STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP800874};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC       {ECO:0000256|PIRNR:PIRNR005727}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC       {ECO:0000256|PIRNR:PIRNR005727}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR005727}. Golgi
CC       apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR005727};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR005727}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane
CC       protein {ECO:0000256|PIRNR:PIRNR005727}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR005727}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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DR   EMBL; JH598179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4B3M5; -.
DR   STRING; 559515.M4B3M5; -.
DR   EnsemblProtists; HpaT800873; HpaP800873; HpaG800873.
DR   EnsemblProtists; HpaT800874; HpaP800874; HpaG800874.
DR   VEuPathDB; FungiDB:HpaG800874; -.
DR   eggNOG; KOG1058; Eukaryota.
DR   HOGENOM; CLU_006949_0_0_1; -.
DR   InParanoid; M4B3M5; -.
DR   OMA; MDYIIPA; -.
DR   Proteomes; UP000011713; Unassembled WGS sequence.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR011710; Coatomer_bsu_C.
DR   InterPro; IPR016460; COPB1.
DR   InterPro; IPR029446; COPB1_appendage_platform_dom.
DR   PANTHER; PTHR10635; COATOMER SUBUNIT BETA; 1.
DR   PANTHER; PTHR10635:SF0; COATOMER SUBUNIT BETA; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF07718; Coatamer_beta_C; 1.
DR   Pfam; PF14806; Coatomer_b_Cpla; 1.
DR   PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR005727};
KW   Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR005727};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|PIRNR:PIRNR005727};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|PIRNR:PIRNR005727};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005727};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR005727};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          27..490
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          710..850
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          856..983
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
SQ   SEQUENCE   1001 AA;  109771 MW;  7D31BA4A328BF73E CRC64;
     MAGVTNERYC TVLLQQVTEE KAVPPSQDEI LKGLESPKVE HKIRAVKSAI LALLQGENLS
     KVLMHIIRFC STQSDHTLKK LLMVYWEIAP KYEQPPPTAA GTTGTAAPPK LLPEMILVCN
     ALLNDLNHPN EYIRGCMLRF LCKIKEKDIL EPLKDAVKSN LEHRHSYVRK NAVMTVYTMY
     KTFGDVVIPD APELIERFIF NESDAGARRN AFLMLNDCAQ DRAVTFLMNA MDQVPKFGDG
     FSLVILETTR KVCRQDPAQK ARFVRCVFQL LNSSSPAVSY EAAWTLVTLS AAPTAVRAAA
     KTYCGLLNSQ SDNNVKLIVL DRLADLKKHH TKVLQEIVMD IMRALSSPSL DICKKVLEIA
     MDLVTVRNID EVVMHLKREV VKTQDKTREK AGEYRHLLIK AIHACAVKFP EVANAVVHLL
     MEFLNQPDGA MDVVVFVRAM CESYPELRKS ILQKLMISFS DISLAKVYRV GLWILGEYAT
     VPLEDGTESD TSIFEAARTI FDAVGSLPLV TEAMLKASAE TVENSAEDPA AATGAAYSKP
     VTKSVVLADG TYATETSYSA PAAKSAVTEE EGVPGLRRLL LSGDFFLGAA VASTLTKLCL
     RVSNGDLANA TAHNAAVKKL VVGCTRCLCA IVAYGQSKAS KHEIDQDSAR RILMGVRVLL
     DPASAQATHA IITEDCRAAY RNLLDAQKAQ EAEAARAAAG GADGEPVSQA DDLINFRQLR
     GKKALGSTDI DIDDGADINR ALGQQGNGAD NEYAGAMRHV HQLTGFADPV YAEAYVTVHD
     YDIVLEILVV NRIPQTLTNL SVDLSTIGDL KLVERPQPQT IGPLDQRTIR ANIKVSSTET
     GHIFGTIVYD SASGAEKTYV NLNDIHLDIM DYIKPATCTD SAFRAMWAEF EWENKVAVHT
     ELSNVFEFLQ HVVDKTNMRC MTPTASLGGD TNFLAANLYA KSVFGEDALV NLSVEKQDSG
     RIAGYIRIRS KTQGIALSLG DRITAVQRGK EDQSKRKKFL A
//
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