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Protein

Alpha-adducin

Gene

Add1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.

GO - Molecular functioni

  • T cell receptor binding Source: RGD

GO - Biological processi

  • cellular response to retinoic acid Source: RGD
  • cytoskeleton organization Source: RGD
  • ion transport Source: RGD
  • negative regulation of actin filament polymerization Source: RGD
  • positive regulation of angiogenesis Source: RGD
  • positive regulation of endocytosis Source: RGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-adducin
Alternative name(s):
Erythrocyte adducin subunit alpha
Gene namesi
Name:Add1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2041. Add1.

Subcellular locationi

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • dendrite Source: RGD
  • dendritic spine Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • postsynaptic density Source: RGD
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Alpha-adducinPRO_0000218532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei59 – 591Phosphoserine; by PKABy similarity
Modified residuei64 – 641PhosphoserineBy similarity
Modified residuei331 – 3311PhosphothreonineBy similarity
Modified residuei334 – 3341PhosphoserineBy similarity
Modified residuei353 – 3531PhosphoserineBy similarity
Modified residuei355 – 3551PhosphoserineCombined sources
Modified residuei358 – 3581PhosphothreonineCombined sources
Modified residuei364 – 3641PhosphoserineBy similarity
Modified residuei366 – 3661PhosphoserineCombined sources
Modified residuei408 – 4081Phosphoserine; by PKABy similarity
Modified residuei427 – 4271PhosphoserineBy similarity
Modified residuei429 – 4291PhosphothreonineBy similarity
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei436 – 4361Phosphoserine; by PKABy similarity
Modified residuei445 – 4451Phosphothreonine; by ROCK2By similarity
Modified residuei464 – 4641PhosphoserineBy similarity
Modified residuei465 – 4651PhosphoserineCombined sources
Modified residuei480 – 4801Phosphothreonine; by ROCK2By similarity
Modified residuei481 – 4811Phosphoserine; by PKABy similarity
Modified residuei586 – 5861PhosphoserineCombined sources
Modified residuei600 – 6001PhosphoserineCombined sources
Modified residuei605 – 6051PhosphoserineBy similarity
Modified residuei610 – 6101PhosphothreonineCombined sources
Modified residuei613 – 6131PhosphoserineBy similarity
Modified residuei614 – 6141PhosphothreonineCombined sources
Modified residuei705 – 7051PhosphoserineBy similarity
Modified residuei708 – 7081PhosphoserineBy similarity
Modified residuei712 – 7121PhosphoserineBy similarity
Modified residuei714 – 7141Phosphoserine; by PKCBy similarity
Modified residuei724 – 7241Phosphoserine; by PKA and PKCBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ63028.
PRIDEiQ63028.

PTM databases

iPTMnetiQ63028.
PhosphoSiteiQ63028.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit or an alpha and a gamma subunit.

GO - Molecular functioni

  • T cell receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018072.

Structurei

3D structure databases

ProteinModelPortaliQ63028.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni715 – 73218Interaction with calmodulinSequence analysisAdd
BLAST

Domaini

Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3699. Eukaryota.
COG0235. LUCA.
HOGENOMiHOG000116349.
HOVERGENiHBG004180.
InParanoidiQ63028.
KOiK18622.
OrthoDBiEOG7HF1HR.
PhylomeDBiQ63028.
TreeFamiTF313003.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
InterProiIPR027766. ADD1.
IPR001303. Aldolase_II/adducin_N.
[Graphical view]
PANTHERiPTHR10672:SF4. PTHR10672:SF4. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q63028-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNGDTRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN
60 70 80 90 100
MMEQKKRVSM ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTA
110 120 130 140 150
SVPNVYPAAP QGGMAALNMS LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA
160 170 180 190 200
AFYRLADLFG WSQLIYNHIT TRVNSEQEHF LIVPFGLLYS EVTASSLVKV
210 220 230 240 250
NLQGDIVDRG STNLGVNQAG FTLHSAIYAA RPDAKCIVHI HTPAGAAVSA
260 270 280 290 300
MKCGLLPISP EALSLGEVAY HDYHGILVDE EEKILIQKNL GPKSKVLILR
310 320 330 340 350
NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLDPGKYK
360 370 380 390 400
AKSRSPGTPA GEGSGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL
410 420 430 440 450
RERSKKYSDV EVPASVTGHS FASDGDSGTC SPLRHSFQKQ QREKTRWLNS
460 470 480 490 500
GRGDDASEEG QNGSSPKSKT KWTKEDGHRT STSAVPNLFV PLNTNPKEVQ
510 520 530 540 550
EMRNKIREQN LQDIKTAGPQ SQVLCGVMMD RSLVQGELVT ASKAIIEKEY
560 570 580 590 600
QPHVIVSTTG PNPFNTLTDR ELEEYRREVE RKQKGSEENL DETREQKEKS
610 620 630 640 650
PPDQSAVPNT PPSTPVKLEG GLPQEPTSRD GSDATTSKPT PPDLSPDEPS
660 670 680 690 700
EALAFPTVAE EAHASPDTTQ PLAEADPEPA SASAPGAEEV ASPATEEGSP
710 720 730
MDPGSDGSPG KSPSKKKKKF RTPSFLKKSK KKSDS
Length:735
Mass (Da):80,355
Last modified:December 1, 2000 - v2
Checksum:i5DFC5DB452774222
GO
Isoform 2 (identifier: Q63028-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     621-632: GLPQEPTSRDGS → GDGCAKEYLLP
     633-735: Missing.

Show »
Length:631
Mass (Da):69,749
Checksum:i42AACB92CFC0D4D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti633 – 6364DATT → GCHA in CAA88907 (PubMed:8543181).Curated
Sequence conflicti654 – 6541A → G in CAA58690 (PubMed:8624703).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti316 – 3161Y → F in strain: Milan hypersensitive.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei621 – 63212GLPQE…SRDGS → GDGCAKEYLLP in isoform 2. CuratedVSP_000179Add
BLAST
Alternative sequencei633 – 735103Missing in isoform 2. CuratedVSP_000180Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49081 mRNA. Translation: CAA88906.1.
Z49082 mRNA. Translation: CAA88907.1.
BC107657 mRNA. Translation: AAI07658.1.
X83715 mRNA. Translation: CAA58690.1.
PIRiS54147.
RefSeqiNP_058686.2. NM_016990.2. [Q63028-1]
UniGeneiRn.5788.

Genome annotation databases

GeneIDi24170.
KEGGirno:24170.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49081 mRNA. Translation: CAA88906.1.
Z49082 mRNA. Translation: CAA88907.1.
BC107657 mRNA. Translation: AAI07658.1.
X83715 mRNA. Translation: CAA58690.1.
PIRiS54147.
RefSeqiNP_058686.2. NM_016990.2. [Q63028-1]
UniGeneiRn.5788.

3D structure databases

ProteinModelPortaliQ63028.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018072.

PTM databases

iPTMnetiQ63028.
PhosphoSiteiQ63028.

Proteomic databases

PaxDbiQ63028.
PRIDEiQ63028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24170.
KEGGirno:24170.

Organism-specific databases

CTDi118.
RGDi2041. Add1.

Phylogenomic databases

eggNOGiKOG3699. Eukaryota.
COG0235. LUCA.
HOGENOMiHOG000116349.
HOVERGENiHBG004180.
InParanoidiQ63028.
KOiK18622.
OrthoDBiEOG7HF1HR.
PhylomeDBiQ63028.
TreeFamiTF313003.

Miscellaneous databases

PROiQ63028.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
InterProiIPR027766. ADD1.
IPR001303. Aldolase_II/adducin_N.
[Graphical view]
PANTHERiPTHR10672:SF4. PTHR10672:SF4. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterisation and chromosomal localisation of the rat alpha- and beta-adducin-encoding genes."
    Tripodi G., Casari G., Tisminetzky S., Bianchi G., Devescovi G., Muro A., Tuteja R., Baralle F.E.
    Gene 166:307-311(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Milan.
    Tissue: Bone marrow.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Spatial and sub-cellular localization of the membrane cytoskeleton-associated protein alpha-adducin in the rat brain."
    Seidel B., Zuschratter W., Wex H., Garner C.C., Gundelfinger E.D.
    Brain Res. 700:13-24(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 426-735.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-355; THR-358; SER-366; SER-465; SER-586; SER-600; THR-610 AND THR-614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADDA_RAT
AccessioniPrimary (citable) accession number: Q63028
Secondary accession number(s): Q3B7D4, Q64722
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 6, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.