ID L5MAM3_MYODS Unreviewed; 543 AA.
AC L5MAM3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=SH2B adapter protein 1 {ECO:0000313|EMBL:ELK35426.1};
GN ORFNames=MDA_GLEAN10007331 {ECO:0000313|EMBL:ELK35426.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK35426.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the SH2B adapter family.
CC {ECO:0000256|ARBA:ARBA00010220}.
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DR EMBL; KB102349; ELK35426.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MAM3; -.
DR eggNOG; ENOG502QT43; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01231; PH_SH2B_family; 1.
DR CDD; cd10346; SH2_SH2B_family; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR030523; SH2B.
DR InterPro; IPR035057; SH2B1_SH2.
DR PANTHER; PTHR10872; SH2B ADAPTER PROTEIN; 1.
DR PANTHER; PTHR10872:SF3; SH2B ADAPTER PROTEIN 1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 283..381
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 13..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 57585 MW; 9EFBCA6B8B3EE982 CRC64;
MVQREELLSF MGAEEAAPDP AGVGRGGGAA GPTSGGGGQP QWQKCRFLLR SEGEGGGGSR
LEFFVPPKAS RPRLSIPCST ITDVRATTAL EMPDRENTFV VKVEGSSEYI LETADALHVK
AWVSDIQECL SPGPCPATSP HPMTLPLAPG ASFLTRENTD SLELPCLNHS ESLPSQDLLL
GPSESNDRLL GQGAYGGLSD RPSASISPSS ASIAASHFDS MELLPPELPP RIPIEEEPPA
GTVHPLSTPY PSLDTPETAT GSFLFQGESE GGEGEQPLSG YPWFHGMLSR LKAAQLVLAG
GTDSHGVFLV RQSETRRGEY VLTFNFQGKA KHLRLSLNEE GQCRVQHLWF QSIFDMLKHF
RVHPIPLESG GPSDVVLGSY VVSSQRQQGR EQAGNHAGVC EGDRCYPDAS STLMPFGAKP
NTSHDPPPPP EPPSWTDPPH PGAEEASGMS EVAAATATAA KERQEKEKVG SGGIQEELVP
VVELVPVVEL EEALTPGMEV RGGPGSGGVP EATPMVQLQQ LPLGGDGEEG GHPRAINNQY
SFV
//