SHLB2_BOVIN
ID SHLB2_BOVIN Reviewed; 395 AA.
AC Q08DK5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Endophilin-B2;
DE AltName: Full=SH3 domain-containing GRB2-like protein B2;
GN Name=SH3GLB2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
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DR EMBL; BC123698; AAI23699.1; -; mRNA.
DR RefSeq; NP_001070270.1; NM_001076802.1.
DR AlphaFoldDB; Q08DK5; -.
DR SMR; Q08DK5; -.
DR STRING; 9913.ENSBTAP00000014049; -.
DR PaxDb; Q08DK5; -.
DR PRIDE; Q08DK5; -.
DR GeneID; 504750; -.
DR KEGG; bta:504750; -.
DR CTD; 56904; -.
DR eggNOG; KOG3725; Eukaryota.
DR HOGENOM; CLU_043817_1_1_1; -.
DR InParanoid; Q08DK5; -.
DR OrthoDB; 803053at2759; -.
DR TreeFam; TF313281; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR CDD; cd11944; SH3_Endophilin_B2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035640; Endophilin_B2_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..395
FT /note="Endophilin-B2"
FT /id="PRO_0000285843"
FT DOMAIN 24..287
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 335..395
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..27
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250"
FT COILED 116..132
FT /evidence="ECO:0000255"
FT COILED 206..240
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR46"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR46"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PPJ9"
SQ SEQUENCE 395 AA; 44051 MW; CE6F3FFB22FAFD0A CRC64;
MDFNMKKLAS DAGIFFTRAV QFTEEKFGQA EKTELDAHFE SLLARADSTK NWTEKILRQT
EVLLQPNPSA RVEEFLYEKL DRKVPSRVTN GELLAQYMAE AASELGPTTP YGKTLIKVAE
AEKHLGAAER DFIHTASINF LTPLRNFLEG DWKTISKERR LLQNRRLDLD ASKARLKKAK
AAEAKATTVP DFQETRPRNY ILSASASALW NDEVDKAEQE LRVAQTEFDR QAEVTRLLLE
GISSTHVNHL RCLHEFIESQ TTYYAQCYRH MLDLQKQLGR FPGTFVGTAE PASPPLSSTS
PTTTAATMPM GPSVADLAPP GEAALRLEEV APPASGTRKA RVLYDYEAAD SSELALLADE
LITVYSLPGM DPDWLIGERG NKKGKVPVTY LELLS