EPB41_CANLF
ID EPB41_CANLF Reviewed; 810 AA.
AC Q6Q7P4;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein 4.1;
DE Short=P4.1;
DE AltName: Full=4.1R;
DE AltName: Full=Band 4.1;
DE AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000250|UniProtKB:P11171};
GN Name=EPB41 {ECO:0000250|UniProtKB:P11171};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=15525677; DOI=10.1091/mbc.e04-05-0426;
RA Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T.,
RA Jagadeeswaran R., Benz E.J. Jr.;
RT "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2
RT kinase.";
RL Mol. Biol. Cell 16:117-127(2005).
CC -!- FUNCTION: Protein 4.1 is a major structural element of the erythrocyte
CC membrane skeleton. It plays a key role in regulating membrane physical
CC properties of mechanical stability and deformability by stabilizing
CC spectrin-actin interaction. Recruits DLG1 to membranes. Required for
CC dynein-dynactin complex and NUMA1 recruitment at the mitotic cell
CC cortex during anaphase. {ECO:0000250|UniProtKB:P11171}.
CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower
CC affinity to band III protein. Associates with the nuclear mitotic
CC apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate
CC with contractile apparatus and tight junctions. Interacts with NUMA1;
CC this interaction is negatively regulated by CDK1 during metaphase and
CC promotes for anaphase-specific localization of NUMA1 in symmetrically
CC dividing cells. Interacts with ATP2B1; regulates small intestinal
CC calcium absorption through regulation of membrane expression of ATP2B1
CC (By similarity). {ECO:0000250|UniProtKB:P11171,
CC ECO:0000250|UniProtKB:P48193}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11171}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11171}. Cytoplasm, cell
CC cortex {ECO:0000250|UniProtKB:P11171}.
CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in the C-
CC terminal domain. {ECO:0000250}.
CC -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC each phosphorylation event selectively modulates the protein's
CC functions. {ECO:0000250}.
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DR EMBL; AY553843; AAS59144.1; -; mRNA.
DR RefSeq; NP_001003362.1; NM_001003362.1.
DR RefSeq; XP_013962011.1; XM_014106536.1.
DR AlphaFoldDB; Q6Q7P4; -.
DR BMRB; Q6Q7P4; -.
DR SMR; Q6Q7P4; -.
DR STRING; 9612.ENSCAFP00000041578; -.
DR PaxDb; Q6Q7P4; -.
DR GeneID; 442955; -.
DR KEGG; cfa:442955; -.
DR CTD; 2035; -.
DR eggNOG; KOG3527; Eukaryota.
DR InParanoid; Q6Q7P4; -.
DR OrthoDB; 262540at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
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 GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:1904478; P:regulation of intestinal absorption; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR021187; Band_41_protein_chordates.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
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:SF12; PTHR23280:SF12; 2.
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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Calmodulin-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Glycoprotein; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..810
FT /note="Protein 4.1"
FT /id="PRO_0000219389"
FT DOMAIN 211..492
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..659
FT /note="Spectrin--actin-binding"
FT REGION 660..810
FT /note="C-terminal (CTD)"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48193"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 223
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48193"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 805
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
SQ SEQUENCE 810 AA; 90688 MW; 8F033CCA3C157602 CRC64;
MTTEKSLVAE AENSQHQQQK EEGEGVTNSG QQETQLEELS QEAAEGDNHC EQKLKTSNGD
TPTHEDLTKN KERTSENRGL SRLFSSFLKR PKSQVSEEEG KDVESAKEKC EGGQKEIEFG
TSLDEEIILK APIAAPEPEL KTDPSLDLHS LSSAETQPAQ EEHREDPDFE TKEGGGLEEC
SKIEVKEESP ESKAERELKA SQKSIRRHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV
CEHLNLLEED YFGLAIWDNG ASKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED
ITRYYLCLQL RQDIVSGRLP CSFATLALLG SYTIQSELGD YDPELHGAEY VSDFKLAPNQ
TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG
LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV
CVEHHTFFRL TSTDTLPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA
SRSLDGAAAV DSDRSPRPTS APAIAQSQDA EGTVPGAPVK KTVVSKAQKE TVKDEEKKEE
GPPDQAEPEP TEVWKDLDKS QEEIKKHHAS ISELKKNFME SVPEPRPSEW DKRLSTHSPF
RTLNINGQLP TGEGPPLVKT QTVTISDTAN SVKSEIPTKD VPIVHTETKT ITYEAAQTDD
SNGDLDPGVL LTAQTITSET TSSTTTTQIT KTVKGGISET RIEKRIVITG DADIDHDQVL
VQAIKEAKEQ HPDMSVTKVV VHQETEISEE
