ID A0A2I0MWM1_COLLI Unreviewed; 1105 AA.
AC A0A2I0MWM1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Erythrocyte membrane protein band 4.1-like 3, transcript variant X1 {ECO:0000313|EMBL:PKK34067.1};
GN Name=EPB41L3 {ECO:0000313|EMBL:PKK34067.1};
GN ORFNames=A306_00001589 {ECO:0000313|EMBL:PKK34067.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK34067.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK34067.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK34067.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK34067.1}.
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DR EMBL; AKCR02000001; PKK34067.1; -; Genomic_DNA.
DR RefSeq; XP_005515059.1; XM_005515002.1.
DR AlphaFoldDB; A0A2I0MWM1; -.
DR STRING; 8932.A0A2I0MWM1; -.
DR InParanoid; A0A2I0MWM1; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13184; FERM_C_4_1_family; 1.
DR CDD; cd17203; FERM_F1_EPB41L3; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR030691; Band4.1-L3_FERM_F1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FA.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR007477; SAB_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR PANTHER; PTHR23280:SF20; BAND 4.1-LIKE PROTEIN 3; 1.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF04382; SAB; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT DOMAIN 1..282
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 378..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 123564 MW; CD601B148F625B35 CRC64;
MQCKVTLLDG SEYACEVEKR SRGQVLFDKV CEHLNLLEKD YFGLTYRDTE NQKNWLDPAK
EIKKQIRSGA WQFAFNVKFY PPDPAQLSED ITRYYLCLQL RDDIVSGRLP CSFVTLALLG
SYTVQSELGD YDPDEYGSDY VSEFRFAPNH TKELEDKVIE LHKSHRGMTP AEAEMHFLEN
AKKLSMYGVD LHHAKDSEGV EIMLGVCASG LLIYRDRLRI NRFAWPKVLK ISYKRNNFYI
KIRPGEFEQF ESTIGFKLPN HRAAKRLWKV CVEHHTFFRL LLPEAPPKKF LTLGSKFRYS
GRTQAQTRRA SALIDRPAPY FERSSSKRYT MSRSLDGASV NENHEMYMKD SVSAAEVGTG
QYATTKGISQ TNLITTVTPE KKAEEEKDDE EGKKKRAEEV TPISAIRHDT KNSLIKRIQG
ENVYVKHSNL MLEDLDKTQE DLMKHQTNIS ELKRTFLETS TETAVSNEWE KRLSTSPVRL
AARQEEAPMI EPLVPEETKE ETEKSEKLIF LQKGGTTFLE MQPSVIEKKL QEGESAGTLV
TSHQIIIQKS IPSILEGTED WVIIDKIPSE VVDGESKKSL AYKVVTVSSK STFPPEMLKS
STILMQSFED LEGEIQSKEE NKQKMFTLGK SYDTVSGKIV TMTSKAKESE KAVQPSVEAL
QKMEREVQES VKIIPVVAEY EILEPVTDEK ARRGSDVQST KRKLSDSLTP IKEAESQLQS
PEEESLKKTL KMDEDLQLHG TLGSLQLGKA EKHLGSEAAK AGAFARRDKS LSEWRYSREQ
PFTIATAHYV TESSTSKVVT KQSTGEKTLD GSDIFSLIES ARKPTEFIGG VTSTSQSWAQ
KIDTTTSQEI TSSEMKQAAH LPQDVVKKVV QETVVIEERH GPSVQASGDP AKAAGLALDT
VTAVVKGKDG SAETEGAKED KREEAQKALT KQGVVTDAAS SCEQVEEHSM TVHLPGSLER
KSHFESPLVK TETISFSTVS ADGENLEIST KEVPVVHTET KTITYESSQV DCGADSEPGV
LMSAQTITSE TTSTTTTTHI TKTVKGGISE TRIEKRIVIT GDADIDHDQA LAQAIKEAKE
QHPDMSVTKV VVHKETEITP EDGED
//