ID A0A182NCG9_9DIPT Unreviewed; 1309 AA.
AC A0A182NCG9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=MHD domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR005333-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR005333-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR005333-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004283}.
CC -!- SIMILARITY: Belongs to the FCHO family.
CC {ECO:0000256|ARBA:ARBA00011064}.
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DR STRING; 7168.A0A182NCG9; -.
DR EnsemblMetazoa; ADIR005333-RA; ADIR005333-PA; ADIR005333.
DR VEuPathDB; VectorBase:ADIR005333; -.
DR OrthoDB; 2996449at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR CDD; cd09265; AP_Syp1_like_MHD; 1.
DR CDD; cd07648; F-BAR_FCHO; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF15; AT02057P; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51072; MHD; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils}.
FT DOMAIN 3..259
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 999..1267
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 348..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 148..187
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 348..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1309 AA; 142151 MW; E587163231204D2B CRC64;
MTVDFNDYFW GEKNNGYEVL YQNMKYGLSA TKELAEYFRE RSNLEEYNSK LLTKLANKAG
SSGGGTFSPL WIILKSTTER LSELHAQKVQ KLTELVKNVT KYAEDLHKKH KSVKEDESGT
QDAVQAMKES TTAVAKAKDV HNARLQEVEK ARKDNSTKEI EKSEAKLRKH QDDYKALVEK
HNIIKQEFEK KMTITCRRFQ EMEEAHLKQM KEFLSSYMDI VQNNFDLVGQ VHSDLKRQFL
ELTVDKLLEQ FVLNKYTGLE KPELIELDFE NCTAGVGSSA GGPNSHQLLV NTAGTVPIAG
SISPAPSSLA GGLLESPTLS ATSSSQPIAI GTTTTKKESH LRSWFSSSSA AAVPTNSPVN
LSTSPTATSV SSGLRYDGDL SAQQQHQQHH HQQQHHPMSL RAMSPVPSVP NDSSVSSSAQ
STSKQSSKPF YGDLFSFKHH STTPSTNHHP PNLASNGHGS GKQQSPLMKQ QEQQQQESLQ
YQQQLQQEQP QQPASPQQQQ QQQQQKSSRR TTSLLNLFMS NSQGSRDSRD STTSTGAAGG
GRRILSGGGN AAASETGRSS VSSAGATVSA PTSPNDAESG SGGGGDQQMQ QQPGNSFIGR
NPLLRGSKFS GFLRSRREKA KSKKAKKKKD SAENSSAKED NILDGDSKGE ATNADSATNL
QTTSAISSSN VAPTATPEVD EDGYSIQPRE NTWDSATITE KSNNFYSSSD SDSEDEKEEK
KIHVEIKPLN NGAAPISASV DELRATVENL SLSPIGILTS ARRGSSFDPQ QQDRLLRMKR
SKSVSQQIGD NGVGVVCKPS HDLLSLNHSI FQQQQQQQHH QQHQLHQQQQ QQQQQHQPLQ
GHALHHQMSV GNASLLNNNV THLTSPNASN ASTPTTVHPY APLQSPTLSM STSSNNRYAD
LGDIFSEVGD ISISAPASAN LTKLTQRQIP TPTSAGGSSI AIPRPPSRRS EAAVARDRVS
PASQIARADS VGSLEFRSPS VGIGSSRGPS PLTIGMSDTI PLAVAFHEII HAYFKGADES
RCQVKMSGDM MISFPAGIVN VLTNNPNPAK LGFRIKNLQN LDNVLPNKQL VTIDRLQSTS
FSTTLEFNMP VLTATLRRQS EQNPNAPHIN VDILKYQIKA KPGAASCPFQ LVSYWKCEQR
HTDIKIDYKY NCHAMAQPSP LLNVSISVPV DGGVKNVQSK PHSAWQGESN RLVWNFTDIS
QHSESGGVDT LRARLEVGTG PSTPAIIATQ FNCEGTTLSG IEFELAGSGY RLSLVKRRFV
SGKYICEGDG IRTVKTPTPP NVSGVMSPVP FGSSNSKPAD NSSSGGTTG
//
