ID A0A452C691_BALAS Unreviewed; 875 AA.
AC A0A452C691;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Breast cancer anti-estrogen resistance protein 1 {ECO:0000313|RefSeq:XP_028018618.1};
GN Name=BCAR1 {ECO:0000313|RefSeq:XP_028018618.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028018618.1};
RN [1] {ECO:0000313|RefSeq:XP_028018618.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028018618.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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 RefSeq; XP_028018618.1; XM_028162817.1.
DR STRING; 310752.A0A452C691; -.
DR InParanoid; A0A452C691; -.
DR OrthoDB; 2902504at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:UP000261681};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 11..73
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 75..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 94305 MW; 8E3A0372EA811DD7 CRC64;
MRNLQQLNPV YNNVLAKALY DNVAESPDEL SFRKGDIMTV LERDTQGLDG WWLCSLHGRQ
GIVPGNRLKI LVGMHDKKPV GPGPGPPASS ALPQPSLHPP AAQYTPMLPA TYQPQPDSVY
LVPTPSKTQQ GLYQAPGPSP QFQSPPAKQT ATFSKQMPHH PFPSPAPDLY QVPPGPGSPA
QDIYQVPPSA GIGHDIYQVP PSMDARSWEG TKPPAKVAVS TRVGQGYVFE APQPEQDEYD
IPRHLLAPGP QDIYDVPPVR GLLPSQCGQE VYDTPPMAVK GPSGRDPSLA VYDVPPSVEK
GLSPSSLHAV YDVPPSVSKD VPDGPLLREE TYDVPPAFAK AKPFDPTRHP LVLAAPPPDS
PPAEDVYDVP PPAPDLYDVP PGLRRPGPGT LYDVPRERVL PPEAANGSVA DDGVYAVPPP
AEREAPADAK RLSASXXXXX XXXXXXXXXX XXXXXXXXXX XXVAVEALAR LQQGVSATVA
HLLDLAGSAG GCEGWRSTSE PQEPPAQDLR AAVAAVHGAV HELLEFARSA VGNAAHTSDR
TLHAKLSRQL QKMEDVYQAL VAHGQALDSS RGGLGATPED LDRLVACSRA VPEDVKQLAS
FLHGNASLLF RRTKASVPGP EGGGPLHPNP TDKASSIQSR PLPSPPRFTS QDSPDGQYEN
SEGGWMEDYD YVHLQGKEEF EKTQKELLEK GNIMRQGKGQ LELQQLKQFE RLEQEVSRPI
DHDLANWMPA QPLAPGRTGG LGPSDRQLLL FYLEQCEANL TTLTNAVDAF FTAVATNQPP
KIFVAHSKFV ILSAHKLVFI GDTLSRQAKA ADVRSQVTHY SNLLCDLLRG IVATTKAAAL
QYPSPAAAQD MVDRVKELGH STQQFRRVLG QLAAA
//
