BI2L2_DANRE
ID BI2L2_DANRE Reviewed; 516 AA.
AC Q1LWE6; Q1LWD6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2;
DE Short=BAI1-associated protein 2-like protein 2;
GN Name=baiap2l2; ORFNames=si:dkey-205o12.6, si:dkey-232h18.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Phosphoinositides-binding protein that induces the formation
CC of planar or gently curved membrane structures. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The IMD domain is predicted to have a helical structure. It may
CC induce actin bundling and filopodia formation (By similarity).
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571946; CAK10744.1; -; Genomic_DNA.
DR EMBL; BX571961; CAK05382.1; -; Genomic_DNA.
DR RefSeq; NP_001074273.1; NM_001080804.1.
DR AlphaFoldDB; Q1LWE6; -.
DR SMR; Q1LWE6; -.
DR STRING; 7955.ENSDARP00000122562; -.
DR PaxDb; Q1LWE6; -.
DR PRIDE; Q1LWE6; -.
DR GeneID; 564798; -.
DR KEGG; dre:564798; -.
DR CTD; 564798; -.
DR ZFIN; ZDB-GENE-060503-339; baiap2l2b.
DR eggNOG; ENOG502QW6V; Eukaryota.
DR InParanoid; Q1LWE6; -.
DR OrthoDB; 457637at2759; -.
DR PhylomeDB; Q1LWE6; -.
DR Reactome; R-DRE-9035034; RHOF GTPase cycle.
DR PRO; PR:Q1LWE6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd11914; SH3_BAIAP2L2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR030126; Pinkbar.
DR InterPro; IPR035593; Pinkbar_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF5; PTHR14206:SF5; 1.
DR Pfam; PF08397; IMD; 2.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipid-binding; Membrane; Reference proteome; SH3 domain.
FT CHAIN 1..516
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2-like protein 2"
FT /id="PRO_0000256132"
FT DOMAIN 1..227
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 274..337
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 200..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 345
FT /note="I -> M (in Ref. 1; CAK05382)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="N -> H (in Ref. 1; CAK05382)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="L -> S (in Ref. 1; CAK05382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 57588 MW; BD857996A6BE745C CRC64;
MSGVNSDLLH RSTLSVYNNL MDQFNPGLQK LVTLGNSYIK AFQALALTSE AYFSALAKMG
EQALSTLSSR SLGDVLIQIS ETQRKLTAEA EGVFRWFHVE VLQAMDKNVK LDEEYIEGSR
RVYELEVRNQ AASLERQLRR GAFRDSLESS EYMQYLRQSQ HEILKEEERR YRFLAEKHCG
LTQSLLYLIN KTGVSLQQRA DGWKEKVSES RSSRPRTPTP LDQEAQLKSS VGSLLQTGDR
EMDREPLGRV PSRAPSPLPS RSRSSSVGES LGLGGGRSMR AIVSHPASSN PVLLPFARGD
LLTVLIPEPR NGWLYGRHDP SLRQGWFPAA YVASTEDFLP VGLSISHRSH SMNNLLEPTS
QSESDTQTYS EVSSPVVSMR RASADVRSVS PLPEKKTESN NELKSGQKVF HEIPAPATQL
RRGSADVRSI SPLPDRRAES HFESKVELKN YNELPPPAPP LPNSPLPERK TDLTSERPST
QGQPPEHPLF PRGSNPFATV KLRPTVTNDR SAPRIQ
