ID A0A182F796_ANOAL Unreviewed; 1038 AA.
AC A0A182F796;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|ARBA:ARBA00017024, ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|ARBA:ARBA00030841, ECO:0000256|PIRNR:PIRNR005727};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB002355-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB002355-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB002355-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) 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 AlphaFoldDB; A0A182F796; -.
DR STRING; 7167.A0A182F796; -.
DR EnsemblMetazoa; AALB002355-RA; AALB002355-PA; AALB002355.
DR VEuPathDB; VectorBase:AALB002355; -.
DR VEuPathDB; VectorBase:AALB20_032124; -.
DR Proteomes; UP000069272; Chromosome 2R.
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|PIRNR:PIRNR005727};
KW Golgi apparatus {ECO:0000256|PIRNR:PIRNR005727};
KW Membrane {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..548
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 670..811
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 816..945
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
SQ SEQUENCE 1038 AA; 116513 MW; E16ADC7B56D042E5 CRC64;
MASVSEGMWC YTIINPPETE TYNEMQLKQD LEKGEVNVKI DTLKKVIQLL LQGERLPNLL
MTIIRFVLPL QNHTIKKLLL IYWEIVPKTS ADGKLLQEMI LVCDAYRKDL QHPNEFLRGS
TLRFLCKLRE PELLEPLMPA IRACLEHRHS YVRRNAVLAI FTIYKNFDWL VPDGPELIAT
FLDTQQDMSC KRNAFLMLLH ADQERALNYL ASCLDQVNSF GDILQLVIVE LIYKVCHANP
AERSRFIRCI YNLLNSSSNA VRYEAAGTLV TLSTAPTAIK AAVSCYIELI VKESDNNVKL
IVLDRLIALK ENENIERIMQ ELVMDVLRVL SATDIEVRRK TLALAMDLVS SRNIEEMVLV
LKKEVSKTHN VEHEDTGKYR QLLVRTLHSC CIKFPDVAAT VIPVLVEFLS DSNELAAGDV
LVFVREAIQK FSHLQPLVIE KLLESFPAIK SSKIHRTTLW ILGEYANSVQ DVMEVIGMIN
RTLGEVPIVE AEQARLDGND AEEEQKKAAE VVNNTNTKVT SDGTYATQSA FSVAPVTKKV
ARPPLRQYLM DGDFFVGATL ATTLTKLALK FLRLEPNEKK QNRVCSCAML VMSSILHLGK
SGLPTKAITN DDIDRIYLCL KTLSLRTPEI VDIFVASCRE SLASMLSAQN DEKLQAQKDK
QQKHAAKIQP DDPISFTQLA DGKNDQLGEN VFELSLNQAL AGTKPTGLTD VASLNSKLNK
ITQLTGFSDP VYAEAYVHVN QYDIVLDVLI VNQTNDTLQN CTLELATVGD LRLVEKPHPV
VLAPNDFCNI KANVKVSSTE NGIIFGNIVY DTTFSSNVVD LNTIQIDIMD YILPATCTDT
EFRSMWVEFE WENKVSVNTT LTDLHDYLRL LLNSTNMRCL TPEKALSGQC GFMAANMYAR
SIFGEDALAN LSIEKSLDRP DAPVTGHIRI RAKSQGMALS LGDKINHTQN IEQTLSILTL
IVSAPLEVVR LYLGYTGNLM STSIATGTLA LQVVLGVPAM RKLSDFRRAQ FQQQRWQYMD
KRSQFFRNKN SKSFDGAC
//