ID   A0A1W4WTE1_AGRPL        Unreviewed;      1025 AA.
AC   A0A1W4WTE1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Spindle pole body component 110 isoform X2 {ECO:0000313|RefSeq:XP_018327159.1};
GN   Name=LOC108738292 {ECO:0000313|RefSeq:XP_018327159.1};
OS   Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC   Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX   NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018327159.1};
RN   [1] {ECO:0000313|RefSeq:XP_018327159.1}
RP   IDENTIFICATION.
RC   TISSUE=Entire body {ECO:0000313|RefSeq:XP_018327159.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ric-3 family.
CC       {ECO:0000256|ARBA:ARBA00008538}.
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DR   RefSeq; XP_018327159.1; XM_018471657.1.
DR   AlphaFoldDB; A0A1W4WTE1; -.
DR   EnsemblMetazoa; XM_018471657.1; XP_018327159.1; LOC108738292.
DR   GeneID; 108738292; -.
DR   OrthoDB; 3716200at2759; -.
DR   Proteomes; UP000192223; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR026160; Ric3.
DR   InterPro; IPR032763; RIC3_N.
DR   PANTHER; PTHR21723; RESISTANCE TO INHIBITORS OF CHOLINESTERASE PROTEIN 3 RIC3; 1.
DR   PANTHER; PTHR21723:SF3; RIC3 ACETYLCHOLINE RECEPTOR CHAPERONE, ISOFORM C; 1.
DR   Pfam; PF15361; RIC3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          166..318
FT                   /note="Resistance to inhibitors of cholinesterase protein 3
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15361"
FT   REGION          179..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1003..1025
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          888..922
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        370..385
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..971
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1025
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1025 AA;  114660 MW;  692B39994CACFD33 CRC64;
     MSETDLGPRK TLFVIVIVVG CFAVLWPKVF YPMLVGPTHK THDYDRGCCD VFSDTDVNTI
     KIISELCSII AQQSDGKKKL TNQEIASNCR NAILSKCGID ISPILNENVY LDGKVKGVLE
     KIRSLNGSLC LKYQFNVSPW VLGVPHKTTT NFTIYNVRQE RPTHLRPEML HPALRERGRA
     IPASSAPRKS PPPKIVEGRP RPIPGMRPPM GGAGHVVPPP QKGTSISIIM PIYTVGIVVF
     FAYTLIKVIF KKKPEGPGFG LYPSVEPDRL FRKQVFESNK NQLKSKYGRD LSGKLDDDEL
     DLLRRRLRET ELAMERIMAQ MAQVPLGSQN HTSNGSVPGT KQDQTSVKVL GMETTASCEG
     GQKWSRPNSP IISPTPPPPV EEPDPPQEIY LEGALPAQSQ LLVSDSKTET QPNTDASDDP
     AVVLASKMTL SVISLDSLPE TENGSSSSSG KDREEYEFVS KSDLSSTQHE DERESQKIPL
     NLKEEFSRDL LQAENISEGE ISNDEVDIEI DDEIDYHKEE DVREIAPDDS VTQTIQEKIN
     NANQNIQNIE KFESKVPIFT DKEKHVDVLN DDIQNANESK VGEEVKVVTP ILHEESHNDT
     EKLPASIEEK STPEVLNREE KHSQELSIQE KIGEENNKTL NFDLQEILKV EEVRDAIDLN
     LNGPNEKQKL INFDLQGDFN VDKPVEVQVQ GYLNLDKPFE VKALQEHEAF GVEDNTIAVK
     LPQNESSTTF EVTAANNEQQ IKNKEDKTLE NRTKETEAEL TQMATEIIDE ITNAAKATFE
     LNNSPSRAVV EVQPILDDDE IFSKYVARVG SDKPIIETSS KKPTTLLLES EISETIQDVS
     SLNNESDQAS EKGSRSLKLS PQGEIIEENY FTLEGSPLSA EEGKSDDMLV VEEVVELSDE
     EYERLERELE EREREREGKI ETSTGVASLI SKQEGETDLK LKGKITSVES AKDLTSDITE
     EDKSGTKENV TDLDEDNDDD LNDFDFNKEL ERIKREMSAF GITVDENDES NEAEKDVKNR
     DQPQV
//