ID A0A329SMF2_9STRA Unreviewed; 993 AA.
AC A0A329SMF2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN ORFNames=PC110_g5882 {ECO:0000313|EMBL:RAW37880.1}, PC113_g7490
GN {ECO:0000313|EMBL:KAG2861054.1}, PC115_g17015
GN {ECO:0000313|EMBL:KAG2897861.1}, PC117_g18652
GN {ECO:0000313|EMBL:KAG2913174.1}, PC118_g1071
GN {ECO:0000313|EMBL:KAG2998944.1}, PC129_g16110
GN {ECO:0000313|EMBL:KAG3212944.1};
OS Phytophthora cactorum.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW37880.1, ECO:0000313|Proteomes:UP000251314};
RN [1] {ECO:0000313|EMBL:RAW37880.1, ECO:0000313|Proteomes:UP000251314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10300 {ECO:0000313|EMBL:RAW37880.1,
RC ECO:0000313|Proteomes:UP000251314};
RA Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG3212944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=15-7 {ECO:0000313|EMBL:KAG2861054.1}, 4032
RC {ECO:0000313|EMBL:KAG2897861.1}, 4040 {ECO:0000313|EMBL:KAG2913174.1},
RC P415 {ECO:0000313|EMBL:KAG2998944.1}, and P421
RC {ECO:0000313|EMBL:KAG3212944.1};
RA Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT "Effector identification in a new, highly contiguous assembly of the
RT strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RAW37880.1}.
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DR EMBL; RCMG01000165; KAG2861054.1; -; Genomic_DNA.
DR EMBL; RCMI01000780; KAG2897861.1; -; Genomic_DNA.
DR EMBL; RCMK01000764; KAG2913174.1; -; Genomic_DNA.
DR EMBL; RCML01000012; KAG2998944.1; -; Genomic_DNA.
DR EMBL; RCMV01000784; KAG3212944.1; -; Genomic_DNA.
DR EMBL; MJFZ01000101; RAW37880.1; -; Genomic_DNA.
DR STRING; 29920.A0A329SMF2; -.
DR Proteomes; UP000251314; Unassembled WGS sequence.
DR Proteomes; UP000697107; Unassembled WGS sequence.
DR Proteomes; UP000735874; Unassembled WGS sequence.
DR Proteomes; UP000736787; Unassembled WGS sequence.
DR Proteomes; UP000760860; Unassembled WGS sequence.
DR Proteomes; UP000774804; 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:UP000251314};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 27..501
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 702..842
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 848..975
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
SQ SEQUENCE 993 AA; 109277 MW; 2E698FC3C63CF5ED CRC64;
MAGVTNERYC TVLLQQVTGE KALPPSQDEI LKGLESPKVE LKIRAVKSAI LALLQGEKLP
KVLMHIIRFC STQSDHTLKK LLMVYWEIAP KYEQQQPGDT SKAPPKLLPE MILVCNALLN
DLNHPNEYIR GCMLRFLCKI KEKDILEPLK DAVKSNLEHR HSYVRKNAVM TVYTMYKTFG
DVLIPDAPEL IERFILNESD AGARRNAFIM LNDCAQDRAV TFLMNAMDQV PKFGDGFSLV
ILEMTRKVCR QDPAQKARFV RCVFQLLNSS SPAVSYEAAW TLVTLSAAPT AVRAAAKTYC
GLLNSQSDNN VKLIVLDRLA DLKKHHTKVL QEILMDIMRA LSSPNLDICK KVLEIAMDLV
SVRNIDEVVT HLKREVVKTQ DKTREKAGEY RHLLIKAIHA CAVKFPEVAN AVVHLLMEFL
NQPDGAMDVV LFVRAMCESY PELRESILQK LMISFPDISL AKVYRVGLWI LGEYATLPPE
DGTESDTSIF EAASTIFTAI GSLPLATEAM LKAPTENPEG ENPATAGAAY SKPVTKSVVL
ADGTYATETS YAAPATKTAT EEENVPGLRR LVLNGDFFLG AAVASTLTKL CLRVSHGDIA
SATARNAAIK KLVVDSTRCM CAVVAYGQAK TSKHEIDQDS ARRILMGVRV LLDPASAQAT
HAIITEECRA AYRHLLDTQK AQEAEAARAA AGGAGGEPVT QADDLINFRQ LRGKKALGST
DIDIDDGADI NRALGQQGDG SDNEYAGAMR HVHQLTGFAD PVYAEAYVTV HDYDIVLEIL
VVNRIPQTLT NLTVDLSTIG DLKLVERPQP QTIGPLDQRT IRANIKVSST ETGHIFGTIV
YDSASGAEKT YVNLNDIHLD IMDYIKPATC TDAAFRAMWA EFEWENKVAV HTELSNVFEF
LQHVVDKTNM RCMTPTASLG GDTNFLAANL YAKSVFGEDA LVNLSVEKQD SGRIAGYIRI
RSKTQGIALS LGDRITAVQR GKDDQGKRKK LLA
//
