ID L5LAV2_MYODS Unreviewed; 573 AA.
AC L5LAV2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=SHC SH2 domain-binding protein 1-like protein {ECO:0000313|EMBL:ELK23332.1};
DE Flags: Fragment;
GN ORFNames=MDA_GLEAN10017508 {ECO:0000313|EMBL:ELK23332.1};
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:ELK23332.1, 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}.
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DR EMBL; KB113703; ELK23332.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LAV2; -.
DR eggNOG; ENOG502QT5S; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045140; SHCBP1-like.
DR PANTHER; PTHR14695; SHC SH2-DOMAIN BINDING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR14695:SF7; TESTICULAR SPINDLE-ASSOCIATED PROTEIN SHCBP1L; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR SMART; SM00722; CASH; 1.
DR SMART; SM00710; PbH1; 4.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 298..458
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK23332.1"
SQ SEQUENCE 573 AA; 64519 MW; 53D9CA14A71B5FCE CRC64;
EEEPLPSVPE EEEEEEEEEA AAAEAQPLPP VCVSPMRGMW REEKVALFCD QVLRGCKAED
ADEAMSNYLS EKLKLKDKWL GVWKTNPELF FLKYEEASIP FVGILVEATC TPHQSSSSCF
RVTVSVAEPF SSNIANIPRN LVNEVLEELE HSVPLLEVYP VEGQDSDIHD IALALEVVRF
FYDFLWRDWD DEERCDNYTA LIEERINLWC DIQDGTIPGP IAQRFKKTLE KYKNKRVELI
EYQNNIKEDP SAAEAVECWK KYYEIVMLCE LLKMWEDLRL RVHGPFFPRI LRRRKGKRDF
GKTITHIVAK VMTTDMVKDL SSDTFLQQHD DLDLALDSCY SGDTVVIFPG EYQAVNLALL
TDDIIIKGVG KREEIMITSE PSHDSFVVSK AANVKLMHLS LIQQGTVDGI VVVEAGHMTL
ENCVLKCEGT GVCVLTGASL TIKDSEIIGA QGAGVELYPG STATLERNEI HHCNNFRTND
SSKSILGGVN MKVLPAPKLK MTNNHIYNNG YGISILPPTE QFFIVAETCN KGAASGDKKD
ENRLSKVMQN MNLEINDNKM EANLKGDIRI ATN
//
