ID A0A1V4JI71_PATFA Unreviewed; 895 AA.
AC A0A1V4JI71;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein 4.1 {ECO:0000256|ARBA:ARBA00023658};
DE AltName: Full=Band 4.1 {ECO:0000256|ARBA:ARBA00030419};
DE AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000256|ARBA:ARBA00032586};
GN Name=EPB41 {ECO:0000313|EMBL:OPJ71860.1};
GN ORFNames=AV530_020121 {ECO:0000313|EMBL:OPJ71860.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ71860.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ71860.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ71860.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ71860.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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:OPJ71860.1}.
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DR EMBL; LSYS01007350; OPJ71860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JI71; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; cd17105; FERM_F1_EPB41; 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; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR021187; EPB4.1_FERM_F1.
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:SF12; PROTEIN 4.1; 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 PIRSF; PIRSF002304; Membrane_skeletal_4_1; 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 Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 213..494
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 99236 MW; B9400E07D29FACD1 CRC64;
MTTEKGPAAD ADSAQQQQQA REEEGAAEAQ EQEASLEEGA EQTREGQPVA GQKQKASNGD
TAAHEEQSRR ERRASEGRGL SRLFSSFLRR PKSQVSEEDK DTDAPKEAGG DQKELGLGAS
PDEDILVKAP IAAPEPELKT DPSLDLHSLS SAETQPAQEE RRDEQEPEGR APGDKDGGEP
EEEGAEPRPE PAETKAEKDL KAAQRAAKRH RNMYCKVVLL DDTIFECAVD KHAKGQELLK
KVCDHLNLLE EDYFGLAVWD TPTSRTWLDP AKEIKKQVHG GPWDFTFNVK FYPPDPAQLT
EDITRYYLCL QLRQDILAGR LPCSFATLAL LGSYTVQSEL GDYDPDLHGP DYIGEFKLAP
NQTKELEEKV VELHKTYRSM TPAQADLEFL ENAKKLSMYG VDLHQAKDLE GVDITLGVCS
SGLLVYKDKL RINRFPWPKV LKISYKRSSF FIKIRPGEQE QYESTIGFKL PSYRAAKKLW
KVCVEHHTFF RLSSTEAIPK SRFLALGSKF RYSGRTQAQT RQASALIDRP APQFERTASK
RASRSLDGAV AVITPERSPR PTSAPAIAQS HAAEPGPAKP GSKDVVAASK IEKEAAKPDV
RREEIPLEKA KPEPADASKV RKTHIAVTVP TANGDQPQQP PAEKEEELIR MRKKRSKRLD
GENIYIRHSN LMLEDLDKTQ EEIKKHHANI SELKKNFMES VPEPRPSEWD KRLSAHSPFR
ALSANGQVPT GADGPPLVKT QTVTLSDVSS ALKSEIPTKE VPIVHTETKT ITYEAAQTDG
GNGDLDPGIL LTAQTITSET TSSTTTTQIT KTVKGGISET RIEKRIVITG DADVDHDQVL
AQAIKAAKEQ HPDMSPGCDA LLPGERHQQN YQETTWSTET SDLQDLTLRD IHITH
//
