ID A0A2Y9GL58_NEOSC Unreviewed; 778 AA.
AC A0A2Y9GL58;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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|RefSeq:XP_021539842.1,
GN ECO:0000313|RefSeq:XP_044770381.1};
OS Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Neomonachus.
OX NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021539842.1};
RN [1] {ECO:0000313|RefSeq:XP_021539842.1, ECO:0000313|RefSeq:XP_044770381.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_021539842.1,
RC ECO:0000313|RefSeq:XP_044770381.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_021539842.1; XM_021684167.1.
DR RefSeq; XP_044770381.1; XM_044914446.1.
DR Proteomes; UP000248481; Chromosome 4.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:UP000248481};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..282
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 308..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 86891 MW; 5F2309765A9D3BF2 CRC64;
MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAVWDNA TSKTWLDSAK
EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVVGRLP CSFATLALLG
SYTIQSELGD YDPELHGADY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN
AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI
KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTLPKSK FLALGSKFRY
SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV DSDRSPRPTS APAIAQSEDT
EVSKAQKETV KVEEQKEEVP PEQAEPEPTE AWKVEKTHIE VTVPTSNGDQ TQKKRERLDG
ENIYIRHSNL MLEDLDKSQE EIKKHHASIS ELKKNFMESV PEPRPSEWDK RLSTHSPFRT
LNINGQLPTG EGNINGIRTE EVAAVTKGPS TNPDSEWDGP KHSVIPSKSQ MTTPSESPQS
FEFGSLSISS KETEEKEQGA AGYLDVKKMP RGSSGECIGV EEQASALKFS VSPASSQLQL
GEKKAESSEE YVTPGEPLGK QNGSFHDSRV GNQFPTLIRS FQPPLVKTQT VTISDTANAV
KSEIPTKDVP IVHTETKTIT YEAAQTDDSN GDLDPGVLLT AQTITSETTS STTTTQITKT
VKGGISETRI EKRIVITGDA DIDHDQVLVQ AIKEAKEQHP DMSVTKVVVH QETEISEE
//
