ID A9V2L9_MONBE Unreviewed; 519 AA.
AC A9V2L9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=F-BAR domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MONBRDRAFT_26520 {ECO:0000313|EMBL:EDQ88281.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ88281.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ88281.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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DR EMBL; CH991555; EDQ88281.1; -; Genomic_DNA.
DR RefSeq; XP_001746874.1; XM_001746822.1.
DR AlphaFoldDB; A9V2L9; -.
DR STRING; 81824.A9V2L9; -.
DR EnsemblProtists; EDQ88281; EDQ88281; MONBRDRAFT_26520.
DR GeneID; 5892262; -.
DR KEGG; mbr:MONBRDRAFT_26520; -.
DR eggNOG; KOG2856; Eukaryota.
DR InParanoid; A9V2L9; -.
DR OMA; EGGNTYN; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR CDD; cd07655; F-BAR_PACSIN; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF11; SYNDAPIN, ISOFORM C; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 35..305
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 400..462
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..385
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 58312 MW; F8645D7A81F53C46 CRC64;
MLQSQPTSIG SGPAAGPRLT PLHDVNAKIA RANKMASAPS FWKVNKYKRV VKRVEDGATL
LDDLKALVHE RAQIERKYAQ MLAAFAKRWE DKIQRGPEEE EGTLRPAWLG LLSEATQLSE
THDKNDERLR TEVADHIADW KKANYKKHMR THKTANDQFV KAQKPWAKLL REMKRSRKAY
YASCEALTAA EDKARGLRRE GAASEDIAKA EAKVAKLTQL KADNRAQYQN NVTALAGDQQ
RYETTMSKAF EFCQDLEQRR QDAFKGFMNT YGRILAGHTP AQCEPLLRDV QAVNPDADLL
AYHKDKGSGM PFPRPVFEDY GAKPTIELVV NKVEDRNSVP LAMKLVDLPS KQCSRKSRRD
NASFGSDEEE EEEDEEEEEE RDWQDDTQWE APPAAAAEEP ILPKMRALYA YQAEDEEELS
LKPGDIIAQV EDEDEQGWCK GVHLGSGKTG IYPALYVEPL PEGADDGDYL EMVGTGVDGL
SSTNVDPEES RRRRLKLYDN YENGTAVSPE APMVPDAVA
//