ID A0A232F313_9HYME Unreviewed; 986 AA.
AC A0A232F313;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=MHD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_008928 {ECO:0000313|EMBL:OXU25144.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU25144.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU25144.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU25144.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU25144.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXU25144.1}.
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DR EMBL; NNAY01001095; OXU25144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232F313; -.
DR STRING; 543379.A0A232F313; -.
DR Proteomes; UP000215335; 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; IPR036168; AP2_Mu_C_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 SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335}.
FT DOMAIN 1..251
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 701..975
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 280..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 156..183
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 324..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 108933 MW; 67E11050E1C7A4BC CRC64;
MTVDFADYFW GEKNNGFDVL YHNMKHGVVA SKELADFLRE RSVIEENNYK LLSKVAKQAS
NSNSTQGTFA PLWAALRGAA EKLAGLHLQL AQRVTELIKD VAKYSDELHK KHKAVKEEES
STLEVVQSIQ SITITLQKTK DTCLQRGLEL EKLRKDNASQ RELEKAEIKF KKAQDDYKNL
VDKYTAIRND FETKMTQSCR RFQDVEETHL RSMKEFLNTY ADVLQSNHEQ VGQVHIDFKR
QCLDMTVDKL LEQFVQSKYT GFEKPGVIEY EEVLTSLAEM TSQTGQEKNS EAPKEISKGA
NGETGVAGNS QALKKIQGGK REGFYTTGRD KSKLHDKEKE KPSERENECV QAQQTKASRR
TTSLLNLFMS NSQERQRQAG SGSAPVSPQE NLSPAVPTPS ISRNPLRGSK WFLRSRREKR
KEKKAKKKKD SVETASNKED KSDPEDKDQD SRKSGTPTPE VDEDGFCIKP KTDPWENEKG
FYSSSDTDSD DERERKIRVE IKPLSNGGAP MSASVDELRA TVENLSLSPA PTGRRGSSTD
SDHHMKRSQS VSQQLGVKPS SDLLNLFNPS STPSSASTPT GSHPYAPLQS PPGLSSSPIP
TMPPPPQSAP PLPRFPEGDL FSELNDVTPA LPPKQSATPT GSSIAIPRPP SRRGDAITRG
RMSPATISRA DSVASLEFRT AGVGVGSSRG PSPLTIGLAD TIPLAVAFHE IIHSYFRGSD
EARCQVKLCG DMMLSFPAGI VAVFATNPNP AKLTFRLKNS NRLERLVPNN TLISMDATQA
TADSTLFEFN MSALTALLRR QAEQNPAASY FNVDILKYQI KNKEGAGSCP FQIVAYWKCN
PTHTDLKVDY KYNSRAMASP TPLLNVQVSV PIDGGFKTVQ SKPNAQWLPD TNRLLWKFTE
LSQHTEGAGV GSLRARVELS RGPGNQGTIF TQFNCEGTTL SGVEFELGGP GYRVSLTKKR
FASGKYLCDG DVDVRTRYAA PPSNVE
//
