ID L5MD33_MYODS Unreviewed; 866 AA.
AC L5MD33;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Breast cancer anti-estrogen resistance protein 1 {ECO:0000313|EMBL:ELK36170.1};
GN ORFNames=MDA_GLEAN10016750 {ECO:0000313|EMBL:ELK36170.1};
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:ELK36170.1, 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: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR EMBL; KB101785; ELK36170.1; -; Genomic_DNA.
DR RefSeq; XP_006755818.2; XM_006755755.2.
DR AlphaFoldDB; L5MD33; -.
DR GeneID; 102751761; -.
DR KEGG; myd:102751761; -.
DR CTD; 9564; -.
DR eggNOG; ENOG502QQHE; Eukaryota.
DR OrthoDB; 2902504at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd11569; FAT-like_BCAR1_C; 1.
DR CDD; cd12001; SH3_BCAR1; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1.
DR Gene3D; 1.20.120.830; Serine-rich domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR046976; BCAR1_C.
DR InterPro; IPR035745; BCAR1_SH3.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654:SF15; BREAST CANCER ANTI-ESTROGEN RESISTANCE PROTEIN 1; 1.
DR PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 3..65
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 66..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 93567 MW; FAFBCAE84FD8B552 CRC64;
MNYLNVLAKA LYDNVAESPD ELSFRKGDIM TVLERDTQGL DGWWLCSLHG RQGIVPGNRL
KILVGMHDKK PAGPGPGPPA PLTPPQPGLH NPAAQYTPML PVAYPPQSDN IYLVPTPSKT
QQGLYQAPGP SPQFQSPPAK QTATFAKQVP HHPFPSPAPD LYQVPPGPGN STQDIYQVPP
SAGIGLDIYQ VPPSMDARSW EGTKPPPKVV VPTRVGQGYV FEASQPEQDE YDIPRHLLGP
GPQDIYDVPP VRGLPSQYSQ EVYDTPPMAV KGPNGWDPSL DVYDVPPSVE KSLPPSSHHA
VYDVPPSVSK DVPDGPLLRE ETYDVPPAFA KAKPFDPTRH PLVLAAPPPD SSPAEDVYDV
PPPAPDIYDV PPGLRRPGPS TLYDVPRERV LPPEVADSSV ADDGVYVVPP SAEREAPADA
KRLSASSTGS TRSSQSASSL ETPVPGREPL ELEVAVEALT RLQQGVSATV THLLDVASSA
GRCGGWRSTT EPQEPPAQDL RAAVAAVQGA VHELLEFARS AVGNSAHTSD RTLNAKLSRQ
LQKMEDVYQT LVAHGQTFDS SRGGPGATSE DLDRLVACSR AVPEDAKQLA SFLHGNASLL
FRRTKAPVSG SEVGGCLHPI PTDKASSIQS RPLPSPPKFT SQDSPDGQYE NSEGGWMEDY
DYVHLQGKEE FEKTQKELLE KGNIIRQGKG QLELQQLKQF ERLEQEVSRP IDHDLTNWTS
AQSLAPGRTG SLGPSDRQLL LFYLEQCEAN LTTLTNAVDA FFTAVATNQP PKIFVAHSKF
VILSAHKLVF IGDTLSRQAK AADVRSQVTH YSNLLCDLLR GIVATTKAAA LQYPSPTAAQ
DMVDRVKELG HSTQQFRRVL GQLAAA
//
