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Database: UniProt
Entry: J9VXU0_CRYNH
LinkDB: J9VXU0_CRYNH
Original site: J9VXU0_CRYNH 
ID   J9VXU0_CRYNH            Unreviewed;       952 AA.
AC   J9VXU0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=CNAG_03299 {ECO:0000313|EMBL:AFR96520.2};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR96520.2, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR96520.2, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
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; CP003827; AFR96520.2; -; Genomic_DNA.
DR   RefSeq; XP_012050909.1; XM_012195519.1.
DR   AlphaFoldDB; J9VXU0; -.
DR   SwissPalm; J9VXU0; -.
DR   GeneID; 23886811; -.
DR   KEGG; cng:CNAG_03299; -.
DR   VEuPathDB; FungiDB:CNAG_03299; -.
DR   HOGENOM; CLU_006949_0_0_1; -.
DR   OrthoDB; 151169at2759; -.
DR   Proteomes; UP000010091; Chromosome 8.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          20..496
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          674..808
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          818..942
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
SQ   SEQUENCE   952 AA;  105618 MW;  FDE4D703AB78747D CRC64;
     MATNAPCYTI VHDDLLDSPS TNDLRNALQK GSDEVKLETM RTIIVGTLNG QSYASLLMPI
     IQYVMPSRSK QLKKMLHFYW EVCPKLDENG KLKQEMILVV NAIRNDLQHP NEYIRGATLR
     YLQKVRESEL LEPLVPTVRQ CLEHRHSFVR KNAVFAVYTI YQDHEHLIPD APELLDTFLA
     AESDSTCKRN AFVTLCNISQ PTAVQYLLNN FDQIESMDEL MQMAVIELVR KEARSEGGHR
     AKWIRCIFEL LNSKSHAVKY EAATSLTTLT QNPAAVKAAA AALAELIVKE ADNNVKLIVL
     DRFNNLRSKH ENVLDGMVMD ILKVLSSPDM EVKRKAIGIA LEMVSSRNVE EVVLFLKKQL
     QGTLDQDFDK NLEYRQLLIQ SIHSCAIRFS EVAANVVYVL MDFLGDSNNP SAVDVIAFVR
     EVVEKFPKLR TAITEKLIST FGEIKSGKVF RGAMWIVGEY CEQPEDIKQA IAEIQKVLGE
     IPILASEQRL LDEAEAADET PAEQQEQPKA ITTTRVLADG TYATETVYTS SASAARLEAV
     RSASKPPLRS LILGGDFFTG SVLASTLTKL VLRYSEVASS DQQSINILRA QAILIMTSVI
     RVGQSKFAAV PIDEDAEERI MNCIETLAEL QGSKALHQVF LKDTKAAYAK MVATEEKKAR
     EKKERESKVS VVQADDLLSF RQLSKKSVVG DVDESDDVVK ATGSIHPQDD FVSKLSRITQ
     LTGFSDPVYA ETVVTLSQYD IILDVLLVNT TNETLQNLMV DFATLGDLKL VERPAPFTLA
     PHGFHSLSAT VKVSSTETGV IFGAITYSKQ GASDADVTIV MSDIHVDIMS FIKPNYVNEA
     QFRSMWTEFE WENKVAVQTS ISDLRAYLDH LLKSTHMALL TPEAALSGDC DFLSANLAAK
     SLFGEDALAN ASIERTEDGH ITGHVRIRSK TQGIALSLGD KITLSQKALV TA
//
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