Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein 4.1

Gene

EPB41

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Calmodulin-binding
Biological processCell cycle, Cell division, Mitosis, Transport

Enzyme and pathway databases

ReactomeiR-CFA-6794361 Neurexins and neuroligins

Names & Taxonomyi

Protein namesi
Recommended name:
Protein 4.1
Short name:
P4.1
Alternative name(s):
4.1R
Band 4.1
Gene namesi
Name:EPB41
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 2

Organism-specific databases

VGNCiVGNC:40392 EPB41

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002193891 – 810Protein 4.1Add BLAST810

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineBy similarity1
Modified residuei61PhosphothreonineBy similarity1
Modified residuei85PhosphoserineBy similarity1
Modified residuei86PhosphoserineBy similarity1
Modified residuei96PhosphoserineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Modified residuei122PhosphoserineBy similarity1
Modified residuei150PhosphoserineBy similarity1
Modified residuei152PhosphoserineBy similarity1
Modified residuei153PhosphoserineBy similarity1
Modified residuei189PhosphoserineBy similarity1
Modified residuei192PhosphoserineBy similarity1
Modified residuei223PhosphotyrosineBy similarity1
Modified residuei379PhosphothreonineBy similarity1
Modified residuei522PhosphoserineBy similarity1
Modified residuei541PhosphoserineBy similarity1
Modified residuei543PhosphoserineBy similarity1
Modified residuei555PhosphoserineBy similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei630PhosphoserineBy similarity1
Modified residuei655PhosphoserineBy similarity1
Modified residuei658PhosphoserineBy similarity1
Modified residuei682PhosphothreonineBy similarity1
Modified residuei805PhosphothreonineBy similarity1

Post-translational modificationi

O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain.By similarity
Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ6Q7P4

Expressioni

Gene expression databases

BgeeiENSCAFG00000011677

Interactioni

Subunit structurei

Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate with contractile apparatus and tight junctions. Interacts with NUMA1; this interaction is negatively regulated by CDK1 during metaphase and promotes for anaphase-specific localization of NUMA1 in symmetrically dividing cells.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000041578

Structurei

3D structure databases

ProteinModelPortaliQ6Q7P4
SMRiQ6Q7P4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini211 – 492FERMPROSITE-ProRule annotationAdd BLAST282

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni615 – 659Spectrin--actin-bindingAdd BLAST45
Regioni660 – 810C-terminal (CTD)Add BLAST151

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi680 – 752Thr-richAdd BLAST73

Phylogenomic databases

eggNOGiENOG410IU7N Eukaryota
ENOG410XS0M LUCA
GeneTreeiENSGT00760000118823
HOVERGENiHBG007777
InParanoidiQ6Q7P4
KOiK06107

Family and domain databases

CDDicd14473 FERM_B-lobe, 1 hit
Gene3Di1.20.80.10, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR008379 Band_4.1_C
IPR019749 Band_41_domain
IPR000798 Ez/rad/moesin-like
IPR014847 FERM-adjacent
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR019747 FERM_CS
IPR000299 FERM_domain
IPR018979 FERM_N
IPR018980 FERM_PH-like_C
IPR011993 PH-like_dom_sf
IPR007477 SAB_dom
IPR029071 Ubiquitin-like_domsf
PfamiView protein in Pfam
PF05902 4_1_CTD, 1 hit
PF08736 FA, 1 hit
PF09380 FERM_C, 1 hit
PF00373 FERM_M, 1 hit
PF09379 FERM_N, 1 hit
PF04382 SAB, 1 hit
PRINTSiPR00935 BAND41
PR00661 ERMFAMILY
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM01195 FA, 1 hit
SM01196 FERM_C, 1 hit
SUPFAMiSSF47031 SSF47031, 1 hit
SSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS00660 FERM_1, 1 hit
PS00661 FERM_2, 1 hit
PS50057 FERM_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q6Q7P4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTEKSLVAE AENSQHQQQK EEGEGVTNSG QQETQLEELS QEAAEGDNHC
60 70 80 90 100
EQKLKTSNGD TPTHEDLTKN KERTSENRGL SRLFSSFLKR PKSQVSEEEG
110 120 130 140 150
KDVESAKEKC EGGQKEIEFG TSLDEEIILK APIAAPEPEL KTDPSLDLHS
160 170 180 190 200
LSSAETQPAQ EEHREDPDFE TKEGGGLEEC SKIEVKEESP ESKAERELKA
210 220 230 240 250
SQKSIRRHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED
260 270 280 290 300
YFGLAIWDNG ASKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED
310 320 330 340 350
ITRYYLCLQL RQDIVSGRLP CSFATLALLG SYTIQSELGD YDPELHGAEY
360 370 380 390 400
VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD
410 420 430 440 450
LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI
460 470 480 490 500
KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTLPKSK
510 520 530 540 550
FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV
560 570 580 590 600
DSDRSPRPTS APAIAQSQDA EGTVPGAPVK KTVVSKAQKE TVKDEEKKEE
610 620 630 640 650
GPPDQAEPEP TEVWKDLDKS QEEIKKHHAS ISELKKNFME SVPEPRPSEW
660 670 680 690 700
DKRLSTHSPF RTLNINGQLP TGEGPPLVKT QTVTISDTAN SVKSEIPTKD
710 720 730 740 750
VPIVHTETKT ITYEAAQTDD SNGDLDPGVL LTAQTITSET TSSTTTTQIT
760 770 780 790 800
KTVKGGISET RIEKRIVITG DADIDHDQVL VQAIKEAKEQ HPDMSVTKVV
810
VHQETEISEE
Length:810
Mass (Da):90,688
Last modified:July 5, 2004 - v1
Checksum:i8F033CCA3C157602
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY553843 mRNA Translation: AAS59144.1
RefSeqiNP_001003362.1, NM_001003362.1
XP_013962011.1, XM_014106536.1
UniGeneiCfa.3914

Genome annotation databases

EnsembliENSCAFT00000013377; ENSCAFP00000012379; ENSCAFG00000011677
GeneIDi442955
KEGGicfa:442955

Similar proteinsi

Entry informationi

Entry namei41_CANLF
AccessioniPrimary (citable) accession number: Q6Q7P4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: March 28, 2018
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health