ID   SHLB2_RAT               Reviewed;         404 AA.
AC   Q5PPJ9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Endophilin-B2;
DE   AltName: Full=SH3 domain-containing GRB2-like protein B2;
GN   Name=Sh3glb2 {ECO:0000312|EMBL:AAH87652.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:AAH87652.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH87652.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB1.
CC       {ECO:0000250|UniProtKB:Q9NR46}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NR46}.
CC   -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH87652.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC087652; AAH87652.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001009692.1; NM_001009692.1.
DR   RefSeq; XP_006233880.1; XM_006233818.3.
DR   AlphaFoldDB; Q5PPJ9; -.
DR   SMR; Q5PPJ9; -.
DR   BioGRID; 260069; 2.
DR   IntAct; Q5PPJ9; 2.
DR   MINT; Q5PPJ9; -.
DR   STRING; 10116.ENSRNOP00000023527; -.
DR   iPTMnet; Q5PPJ9; -.
DR   PhosphoSitePlus; Q5PPJ9; -.
DR   SwissPalm; Q5PPJ9; -.
DR   jPOST; Q5PPJ9; -.
DR   PaxDb; Q5PPJ9; -.
DR   PRIDE; Q5PPJ9; -.
DR   GeneID; 311848; -.
DR   KEGG; rno:311848; -.
DR   UCSC; RGD:1305886; rat.
DR   CTD; 56904; -.
DR   RGD; 1305886; Sh3glb2.
DR   eggNOG; KOG3725; Eukaryota.
DR   InParanoid; Q5PPJ9; -.
DR   OrthoDB; 803053at2759; -.
DR   PhylomeDB; Q5PPJ9; -.
DR   PRO; PR:Q5PPJ9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:UniProt.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
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   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW   SH3 domain.
FT   CHAIN           1..404
FT                   /note="Endophilin-B2"
FT                   /id="PRO_0000307713"
FT   DOMAIN          24..291
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   DOMAIN          344..404
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          1..27
FT                   /note="Membrane-binding amphipathic helix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y371"
FT   COILED          209..239
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         404
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   404 AA;  44853 MW;  8E387EE5AEC33CDE CRC64;
     MDFNMKKLAS DAGIFFTRAV QFTEEKFGQA EKTELDAHFE NLLARADSTK NWTERILRQT
     EVLLQPNPSA RVEEFLYEKL DRKVPSRVTN GELLAQYMAE AASELGPNTP YGKTLMKVSE
     AEKRLGAAER DFIHTASLSF LTPLRNFLEG DWKTISKERR LLQNRRLDLD ACKARLKKAK
     AAEAKATCEG DTVPDFQETR PRNYILSASA SALWNDEVDK AEQELRAAQT EFDRQAEVTR
     LLLEGISSAH VNHLRCLHEF VKSQTTYYAQ CYRHMLDLQK QLGSSQGAIF PGTFVGTTEP
     ASPPLSSTSP TTTAATMPVV PTGAGLAPPE EAALCLEEVA PPASGTRKAR VLYDYEAADS
     SELALLADEL ITVYSLPGMD PDWLIGERGN KKGKVPVTYL ELLS