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Database: UniProt
Entry: M1K742_ENCCN
LinkDB: M1K742_ENCCN
Original site: M1K742_ENCCN 
ID   M1K742_ENCCN            Unreviewed;       818 AA.
AC   M1K742;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=ECU08_1100 {ECO:0000313|EMBL:AGE95017.1};
OS   Encephalitozoon cuniculi (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=6035 {ECO:0000313|EMBL:AGE95017.1};
RN   [1] {ECO:0000313|EMBL:AGE95017.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23376943; DOI=10.1128/EC.00307-12;
RA   Selman M., Sak B., Kvac M., Farinelli L., Weiss L.M., Corradi N.;
RT   "Extremely Reduced Levels of Heterozygosity in the Vertebrate Pathogen
RT   Encephalitozoon cuniculi.";
RL   Eukaryot. Cell 12:496-502(2013).
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; KC513605; AGE95017.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1K742; -.
DR   VEuPathDB; MicrosporidiaDB:AEWD_081090; -.
DR   VEuPathDB; MicrosporidiaDB:AEWQ_081130; -.
DR   VEuPathDB; MicrosporidiaDB:AEWR_081140; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_1100; -.
DR   VEuPathDB; MicrosporidiaDB:M970_081140; -.
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; 2.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          16..188
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          575..674
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          689..805
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
SQ   SEQUENCE   818 AA;  93657 MW;  B8F98FE29170F834 CRC64;
     MQASLYLNTS MRMRKDEIMQ KLRSSSEQDK IEGMKQMIAQ MSQGEDFSSL THKITKETLV
     VRSNELKRLF YYYLELLPKA RGTQSFEEML LLSNQVRKDL EHPNEYVRGF VMRFVSTLDD
     QELVGNFYKL IKDNFNHPNT YVRRNAYFCL GEIFLKMDMY KEVPDLLYHA LLRDLDPNCL
     REAFVSLHLT DPELALKYAG EVSLSIPSEL STAIVEKIKD ERLLERFLFS EDSMTAFEAG
     MSIHRMSNDE QLLKRSTDTI LRCLEDLPRC REYAIDELLL STYSFSGYAM SFLSLIDPYD
     LSFCSKCFDF VFKISETHEF LQISDFLAFR FMDTHDASVQ NQSFRVLLLE KMAYFASTYS
     SYNEEMVSEA LKSIASDNPE MSHASLMFLS SCFEIMSRSS ESCEGDAAGH GSYLEVLVNK
     INEVKYGKIL RCCFGILRRH ATKEIFLRVV EVLESSFGHA DRPLYLRNTQ TFLGAFMCIE
     LSEMCRRLEG PKDRVIAVML RFIEHGKESN TIDMSSQSTI VSCIRSLVSC NSQGEVSSNG
     HKRCREGVLD PIMLPGTRSS DERGLNKLNE FLVDSEGGSA EMRNVTQLTG LSDPIYVEAT
     TSYTRYEIVV DMLFINQTPS YLQNILLDFV TSQGLSATFI STPFSLSSRS VVTKRFTFRI
     IDASNGFISG SITFRYPDEC GEYANTVYTI NLSEVKTSVS EFLEPRKMDP DGFRETWKEL
     EWENTYTLKF ITKKTLEEIF GEVSRVLNGE TLDIECDEDY AVGNIACSTL QNVCVLVNVC
     LRRSEHVHFE SRIRSRKEGI VKSVSAVVGD VLRSLKNK
//
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