P11434 (41_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoskeletal protein 4.1

Alternative name(s):
Band 4.1

Gene names

Name:

epb41

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	801 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Subunit structure	Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Binds calmodulin By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell cortex By similarity. Nucleus By similarity.
Tissue specificity	Found exclusively in photoreceptors following the terminal mitosis of retinal neurons. When retinal synaptogenesis is complete, protein 4.1 is also expressed in the inner retina. In adult amphibian retinas, protein 4.1 is detected in photoreceptors, bipolar cells, and ganglion cell axons.
Post-translational modification	Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	Actin-binding
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cortical actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro
Cellular component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 801	801	Cytoskeletal protein 4.1		PRO_0000219393
Regions
	Domain	193 – 474	282	FERM
	Region	477 – 587	111	Hydrophilic
	Region	588 – 651	64	Spectrin--actin-binding
	Region	653 – 801	149	Carboxyl-terminal (CTD)

Sequences

	Sequence		Length	Mass (Da)
	P11434 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 07FA508552359A0F	FASTA	801	89,429
	10 20 30 40 50 60 MTTEKGLLAE AESPPQDQKQ EGEEEVESCT TQPVVGSGDK DPETEQSQES PSTTSPSTRK 70 80 90 100 110 120 SKDRHSQGKG LSRLFSSFLK RPKSQVSSDE KEVELLGEKG QDQKDVDEGL GEQLEDDVFL 130 140 150 160 170 180 KAPIAAPEPE LRTDPSLDLH SLSSAETQPA QEEQKEDQDP EADCEDVEGK EPIKKPEGES 190 200 210 220 230 240 KASHKVVRRS PNMRCKVTLL DDTVYECDLE KHAKGQDIFK KVCSHLNIVE EDYFGLAIWE 250 260 270 280 290 300 SPTCKVWLDP LKDIRKQVHG GPCEFTSNVK FYPPDPAQLS EDITRYYLCL QLRKDIFSGR 310 320 330 340 350 360 LPCSFATLAL LGSYTVQSEV GDYEEDLHGV DYVSEFKLSP NQTKDLEEKV GELHKSYRSM 370 380 390 400 410 420 TPAQADLEFL ENAKKLTMYG VDIHQAKDLE GVDIKLGVCS GGLMVFKDNL RINRFPWPKV 430 440 450 460 470 480 LKISYKRSSF FIKIRPGEQE QYESTIGFKL PSYKAAKKLW KVCVEHHTFF RLTSTESIPK 490 500 510 520 530 540 HRFLSLGSTF RYSGRTQAQT RHASALIDRP APHFVRTGSK RASRSLDGAA VATPEASRTH 550 560 570 580 590 600 RPVSAPVFPP EFPAVQRKTP GPRVEEMPKK TEEKPKEGMP NQRESPKDVK ATQQDSPSPT 610 620 630 640 650 660 VNGDKVKDLE KTQDEIIRHH ASIRELKKSF MESVPAPRPS EWDKRLSTHS PFRTLSFNGQ 670 680 690 700 710 720 VQTGTDGPPL VKTQTVTISN ATNGEKGEIP TKEVPLVHTE TKTITYEAAR SDDVNTDQEP 730 740 750 760 770 780 GILLTAHTIT SETTSSTTTT QITKTVKGGI SETLIEKRIV ITGDGDLDHD QVLVQAIKEA 790 800 KEQHPDMSVT KGVVHQETEI A

References

[1]	"Membrane skeleton protein 4.1 in developing Xenopus: expression in postmitotic cells of the retina." Spencer M., Giebelhaus D.H., Kelly G.M., Bicknell J., Florio S.K., Bunt-Milam A., Moon R.T. Dev. Biol. 139:279-291(1990) [PubMed: 2186944] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Antisense RNA inhibits expression of membrane skeleton protein 4.1 during embryonic development of Xenopus." Giebelhaus D.H., Eib D.W., Moon R.T. Cell 53:601-615(1988) [PubMed: 2453290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-550.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M20621 mRNA. Translation: AAA49695.1.
PIR	A37353.
RefSeq	NP_001081264.1. NM_001087795.1.
UniGene	Xl.12931.
3D structure databases
ProteinModelPortal	P11434.
SMR	P11434. Positions 193-471.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397741.
KEGG	xla:397741.
Organism-specific databases
CTD	2035.
Xenbase	XB-GENE-865471. epb41.
Phylogenomic databases
HOVERGEN	HBG007777.
Family and domain databases
InterPro	IPR008379. Band_4.1_C. IPR019749. Band_41_domain. IPR019750. Band_41_fam. IPR021187. Band_41_protein. IPR000798. Ez/rad/moesin. IPR014847. FERM-adjacent. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR019747. FERM_CS. IPR000299. FERM_domain. IPR018979. FERM_N. IPR018980. FERM_PH-like_C. IPR011993. PH_type. IPR007477. SAB. [Graphical view]
Gene3D	G3DSA:1.20.80.10. ACBP. 1 hit. G3DSA:2.30.29.30. PH_type. 1 hit.
KO	K06107.
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. [Graphical view]
PIRSF	PIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTS	PR00935. BAND41. PR00661. ERMFAMILY.
SMART	SM00295. B41. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit.
PROSITE	PS00660. FERM_1. 1 hit. PS00661. FERM_2. 1 hit. PS50057. FERM_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

41_XENLA

Accession

Primary (citable) accession number: P11434

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 16, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program