ID A0A182RC00_ANOFN Unreviewed; 960 AA.
AC A0A182RC00;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=PDZ domain-containing protein 8 {ECO:0008006|Google:ProtNLM};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN003715-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN003715-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN003715-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR AlphaFoldDB; A0A182RC00; -.
DR STRING; 62324.A0A182RC00; -.
DR EnsemblMetazoa; AFUN003715-RA; AFUN003715-PA; AFUN003715.
DR VEuPathDB; VectorBase:AFUN003715; -.
DR VEuPathDB; VectorBase:AFUN2_007277; -.
DR OrthoDB; 3681901at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:InterPro.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:InterPro.
DR CDD; cd20825; C1_PDZD8; 1.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR CDD; cd21674; SMP_PDZD8; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR039275; PDZD8.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR21519; PDZ DOMAIN-CONTAINING PROTEIN 8; 1.
DR PANTHER; PTHR21519:SF1; PDZ DOMAIN-CONTAINING PROTEIN 8; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51847; SMP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 5..186
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 254..311
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 619..669
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 378..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 106821 MW; 9516F4A63523F8AC CRC64;
MAINLILQFL YFELRQSNRV RKWFHRKLSL ELDELISKTT TGKLFDKLTI RDLDLGSQFP
EIKNFRLHAV DLHPDEGHIE SLDVLLDLHY EGNFRLTIDA DMVLGKGSLA LRVKQVSGLA
RLQFTRKPYT HWSLSFINDP KVELDVQSHF QGRQMQSNIT SLISNQIRKA IRRKHTLPNY
KLRYKPFFHR VEEDYELNEI VPNGTLEVTI AEISRLNAPI RTLSHVYCTL TLAHMPWVVA
RQQEDQSVMI VSLDIEIHKA KNQQIGIVFK QTEQTVLIDA VIPNTPASKA ELRRGDVLLS
IQGKRVTNIS QVPKVIKTLN RPMFVLRIER LVPGQIKNDG LLEDYEADFE EIDPNLNITF
VKNVEAVQIG SSSTSGTVLR RKLVRRNSKD NSGGESSHSN TPGTTPVKKV AIAGRDSIIP
GMESTPRGSF EPATGGKPKA NVDCYPQHSS VDAEFNSFIR LDDPCTFQLM EKYSYLNLSV
FGKNNEENRL LGYLNIPINS ILVECNESHL GHHLKKYPLL PPEAIDVSNH ALSMQSGFDQ
NYCYGDVLLS FVWNGSALAC STATPSKVIG GENKKQRLIT ISRGSADKLD DDRTDGFLEV
KSPTPTSTQL PPQVQPQQHH DFIRTHFHRT TQCDYCGKKI WLKDAVQCRD CAMCCHKKCI
NKCQSSTVCT ANETAVAATV ERSPSSSTTT TTASGGPVAV TTPASLQPEF KLTEPESPTI
EVEDFVDIAE EQQQIVSKSK LETHRQSFSD LLVQGLKRVN SANNLSIPTM GGMNPSSKSL
PPTPQHTPRK QSLANVSANP FLLVTQRLES LPEDVNELNM EQLVELTAPL IEYGPSDTLM
ALAKSSSKTM YGDCEPDVRT EKINKLLSKL HIALDYETIN QSVLNATKES NSSSGSSGAG
ANPNSKEITD GKGKCAAQQQ HDSTRSAFLA GQSEERVQAL SIIMLHLCSG LQYVQGNLGQ
//
