ID L5M7B5_MYODS Unreviewed; 415 AA.
AC L5M7B5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Myb/SANT-like DNA-binding domain-containing protein 3 {ECO:0000256|ARBA:ARBA00021372};
GN ORFNames=MDA_GLEAN10021524 {ECO:0000313|EMBL:ELK34180.1};
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:ELK34180.1, 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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the MSANTD3 family.
CC {ECO:0000256|ARBA:ARBA00007954}.
CC -!- SIMILARITY: Belongs to the tomoregulin family.
CC {ECO:0000256|ARBA:ARBA00038484}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB103229; ELK34180.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M7B5; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00104; KAZAL_FS; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR028002; Myb_DNA-bind_5.
DR PANTHER; PTHR21632:SF2; MYB_SANT-LIKE DNA-BINDING DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR21632; UNCHARACTERIZED; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF13873; Myb_DNA-bind_5; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 223..270
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 314..354
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 344..353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 415 AA; 46641 MW; D6A4D004D4A7E5DE CRC64;
MQNNEIIKPA KYFSELEKSI LLALVEKYKY VLECKKSDAR TIALKQRTWQ ALAHEYNSQP
SVSLRDFKQL KKCWENIKAR TKKIMAHERR EKVKRSVSPL LSSHVLGKEK IASMLPEQLY
FLQSPPEEEP EYHPDAAAQG RTSSSSRDEG SLENCSPEIC LPRPHLDLEL QETPCSSQSF
SYECQSEANL ELNVRESDVR VCDESSCKYG GVCKEDGDGL KCACQFQCHT NYIPVCASNG
DTYQNECFLR RAACKHQKEI TVVARGPCYS DNGSGSGEGD TDDTSLLGKK DDGLPYRPDV
KDASDQREDV YIGNHMPCPE NLNGYCIHGK CEFIYATQKA SCRCESGYTG QHCEKTDFSI
LYVVPIYTHL LPSQTLGHHS IFLTVLYRIF TTHSAPLPLV ACHVPCHSLV VIASD
//
