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O55017 (CAC1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-dependent N-type calcium channel subunit alpha-1B
Alternative name(s):
Brain calcium channel III
Short name=BIII
Calcium channel, L type, alpha-1 polypeptide isoform 5
Voltage-gated calcium channel subunit alpha Cav2.2
Gene names
Name:Cacna1b
Synonyms:Cach5, Cacnl1a5, Cchn1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1Bgives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.

Subunit structure

Multisubunit complex consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts with RIMS1 and RIMBP2 By similarity. Ref.3

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Widespread expression throughout the brain. Highest levels in pyramidal cell layers C1, C2 and C3 of the hippocampus, in the dentate gyrus, in the cortex layers 2 et 4, in the subiculum and the habenula.

Domain

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.

Post-translational modification

Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK By similarity.

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1B subfamily. [View classification]

Contains 1 EF-hand domain.

Sequence caution

The sequence AAB60437.1 differs from that shown. Reason: Frameshift at positions 1924, 1934, 2121 and 2127.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from mutant phenotype PubMed 12074836. Source: MGI

calcium ion transport

Inferred from mutant phenotype PubMed 11296258PubMed 12827191. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 12890773. Source: MGI

neurotransmitter secretion

Inferred from mutant phenotype PubMed 12827191. Source: MGI

regulation of blood pressure

Inferred from mutant phenotype PubMed 11296258. Source: MGI

regulation of calcium ion transport

Inferred from mutant phenotype PubMed 12074836. Source: MGI

regulation of heart contraction

Inferred from mutant phenotype PubMed 11296258. Source: MGI

response to pain

Inferred from mutant phenotype PubMed 12074836. Source: MGI

   Cellular_componentdendrite

Inferred from direct assay PubMed 15451373. Source: MGI

membrane

Inferred from direct assay PubMed 18054859. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 15451373. Source: MGI

voltage-gated calcium channel complex

Inferred from direct assay PubMed 10328888. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: InterPro

voltage-gated calcium channel activity

Inferred from mutant phenotype PubMed 11296258PubMed 12074836PubMed 12827191. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform NB1 (identifier: O55017-1)

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.
Isoform NB2 (identifier: O55017-2)

The sequence of this isoform differs from the canonical sequence as follows:
     756-756: A → AFVKQTRGTVSRSSSVSSVNSP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23272327Voltage-dependent N-type calcium channel subunit alpha-1B
PRO_0000053922

Regions

Topological domain1 – 9595Cytoplasmic Potential
Transmembrane96 – 11419Helical; Name=S1 of repeat I; Potential
Topological domain115 – 13319Extracellular Potential
Transmembrane134 – 15118Helical; Name=S2 of repeat I; Potential
Topological domain152 – 16413Cytoplasmic Potential
Transmembrane165 – 17915Helical; Name=S3 of repeat I; Potential
Topological domain180 – 1867Extracellular Potential
Transmembrane187 – 20519Helical; Name=S4 of repeat I; Potential
Topological domain206 – 22520Cytoplasmic Potential
Transmembrane226 – 24520Helical; Name=S5 of repeat I; Potential
Topological domain246 – 33186Extracellular Potential
Transmembrane332 – 35625Helical; Name=S6 of repeat I; Potential
Topological domain357 – 482126Cytoplasmic Potential
Transmembrane483 – 50220Helical; Name=S1 of repeat II; Potential
Topological domain503 – 51614Extracellular Potential
Transmembrane517 – 53620Helical; Name=S2 of repeat II; Potential
Topological domain537 – 5448Cytoplasmic Potential
Transmembrane545 – 56319Helical; Name=S3 of repeat II; Potential
Topological domain564 – 57411Extracellular Potential
Transmembrane575 – 59218Helical; Name=S4 of repeat II; Potential
Topological domain593 – 61119Cytoplasmic Potential
Transmembrane612 – 63120Helical; Name=S5 of repeat II; Potential
Topological domain632 – 68453Extracellular Potential
Transmembrane685 – 70925Helical; Name=S6 of repeat II; Potential
Topological domain710 – 1134425Cytoplasmic Potential
Transmembrane1135 – 115824Helical; Name=S1 of repeat III; Potential
Topological domain1159 – 117517Extracellular Potential
Transmembrane1176 – 119520Helical; Name=S2 of repeat III; Potential
Topological domain1196 – 12038Cytoplasmic Potential
Transmembrane1204 – 122623Helical; Name=S3 of repeat III; Potential
Topological domain1227 – 124115Extracellular Potential
Transmembrane1242 – 125615Helical; Name=S4 of repeat III; Potential
Topological domain1257 – 127721Cytoplasmic Potential
Transmembrane1278 – 129720Helical; Name=S5 of repeat III; Potential
Topological domain1298 – 138386Extracellular Potential
Transmembrane1384 – 140825Helical; Name=S6 of repeat III; Potential
Topological domain1409 – 146557Cytoplasmic Potential
Transmembrane1466 – 148419Helical; Name=S1 of repeat IV; Potential
Topological domain1485 – 149814Extracellular Potential
Transmembrane1499 – 151820Helical; Name=S2 of repeat IV; Potential
Topological domain1519 – 15279Cytoplasmic Potential
Transmembrane1528 – 154619Helical; Name=S3 of repeat IV; Potential
Topological domain1547 – 15548Extracellular Potential
Transmembrane1555 – 157319Helical; Name=S4 of repeat IV; Potential
Topological domain1574 – 159219Cytoplasmic Potential
Transmembrane1593 – 161220Helical; Name=S5 of repeat IV; Potential
Topological domain1613 – 167462Extracellular Potential
Transmembrane1675 – 169420Helical; Name=S6 of repeat IV; Potential
Topological domain1695 – 2327633Cytoplasmic Potential
Repeat82 – 359278I
Repeat468 – 712245II
Repeat1126 – 1412287III
Repeat1449 – 1702254IV
Domain1715 – 175036EF-hand
Nucleotide binding451 – 4588ATP Potential
Calcium binding1728 – 173912 By similarity
Region379 – 39618Binding to the beta subunit By similarity
Compositional bias2040 – 20445Poly-His
Compositional bias2106 – 21105Poly-Ser

Sites

Site3141Calcium ion selectivity and permeability By similarity
Site6631Calcium ion selectivity and permeability By similarity
Site13581Calcium ion selectivity and permeability By similarity
Site16461Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue7831Phosphoserine Ref.4
Modified residue17101Phosphoserine; by PKA Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation15541N-linked (GlcNAc...) Potential
Glycosylation16661N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence7561A → AFVKQTRGTVSRSSSVSSVN SP in isoform NB2.
VSP_000883
Natural variant4141D → DA.

Experimental info

Sequence conflict2381A → G in AAB60437. Ref.2
Sequence conflict6451N → I in AAB60437. Ref.2
Sequence conflict757 – 7593RQQ → QE in AAB60437. Ref.2
Sequence conflict8801A → P in AAB60437. Ref.2
Sequence conflict11281L → F in AAB60437. Ref.2
Sequence conflict11731K → E in AAB60437. Ref.2
Sequence conflict11851F → C in AAB60437. Ref.2
Sequence conflict1227 – 12304Missing in AAB60437. Ref.2
Sequence conflict13881F → L in AAB60437. Ref.2
Sequence conflict15491A → AET in AAB60437. Ref.2
Sequence conflict16151I → S in AAB60437. Ref.2
Sequence conflict16361L → I in AAB60437. Ref.2
Sequence conflict16571G → D in AAB60437. Ref.2
Sequence conflict1802 – 183736Missing in AAB60437. Ref.2
Sequence conflict19421A → G in AAB60437. Ref.2
Sequence conflict19491G → D in AAB60437. Ref.2
Sequence conflict19631A → L in AAB60437. Ref.2
Sequence conflict19791E → D in AAB60437. Ref.2
Sequence conflict19941P → L in AAB60437. Ref.2
Sequence conflict20211H → D in AAB60437. Ref.2
Sequence conflict20751A → AA in AAB60437. Ref.2
Sequence conflict21411T → A in AAB60437. Ref.2
Sequence conflict21681S → I in AAB60437. Ref.2
Sequence conflict23091S → N in AAB60437. Ref.2
Sequence conflict23131R → G in AAB60437. Ref.2
Sequence conflict23161H → A in AAB60437. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform NB1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: AD42CDD38482895A

FASTA2,327261,481
        10         20         30         40         50         60 
MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN 

        70         80         90        100        110        120 
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD 

       130        140        150        160        170        180 
GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA 

       190        200        210        220        230        240 
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII 

       250        260        270        280        290        300 
GLEFYMGKFH KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP NFGITNFDNI 

       310        320        330        340        350        360 
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA 

       370        380        390        400        410        420 
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDVLKRAA 

       430        440        450        460        470        480 
TKKSRNDLIH AEEGEDRFVD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK 

       490        500        510        520        530        540 
AQSFYWVVLC VVALNTLCVA MVHYNQPQRL TTALYFAEFV FLGLFLTEMS LKMYGLGPRS 

       550        560        570        580        590        600 
YFRSSFNCFD FGVIVGSIFE VVWAAIKPGT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV 

       610        620        630        640        650        660 
SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL 

       670        680        690        700        710        720 
TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK 

       730        740        750        760        770        780 
DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN SAKARSVWEQ RASQLRLQNL 

       790        800        810        820        830        840 
RASCEALYSE MDPEERLRYA STRHVRPDMK THMDRPLVVE PGRDGLRGPV GSKSKPEGTE 

       850        860        870        880        890        900 
ATESADLPRR HHRHRDRDKT SATAPAGGEQ DRTESTETGA REERARPRRS HSKETPGADT 

       910        920        930        940        950        960 
QVRCERSRRH HRRGSPEEAT EREPRRHRAH RHAQDSSKEG TAPVLVPKGE RRARHRGPRT 

       970        980        990       1000       1010       1020 
GPREAENNEE PTRRHRARHK VPPTLQPPER EAAEKESNAV EGDKETRNHQ PKEPHCDLEA 

      1030       1040       1050       1060       1070       1080 
IAVTGVGPLH MLPSTCLQKV DEQPEDADNQ RNVTRMGSQP SDPSTTVHVP VTLTGPPGET 

      1090       1100       1110       1120       1130       1140 
PVVPSGNMNL EGQAEGKKEA EADDVLRRGP RPIVPYSSMF CLSPTNLLRR FCHYIVTMRY 

      1150       1160       1170       1180       1190       1200 
FEMVILVVIA LSSIALAAED PVRTDSFRNN ALKYMDYIFT GVFTFEMVIK MIDLGLLLHP 

      1210       1220       1230       1240       1250       1260 
GAYFRDLWNI LDFIVVSGAL VAFAFSSFMG GSKGKDINTI KSLRVLRVLR PLKTIKRLPK 

      1270       1280       1290       1300       1310       1320 
LKAVFDCVVN SLKNVLNILI VYMLFMFIFA VIAVQLFKGK FFYCTDESKE LERDCRGQYL 

      1330       1340       1350       1360       1370       1380 
DYEKEEVEAQ PRQWKKYDFH YDNVLWALLT LFTVSTGEGW PMVLKHSVDA TYEEQGPSPG 

      1390       1400       1410       1420       1430       1440 
FRMELSIFYV VYFVVFPFFF VNIFVALIII TFQEQGDKVM SECSLEKNER ACIDFAISAK 

      1450       1460       1470       1480       1490       1500 
PLTRYMPQNK QSFQYKTWTF VVSPPFEYFI MAMIALNTVV LMMKFYDAPY EYELMLKCLN 

      1510       1520       1530       1540       1550       1560 
IVFTSMFSME CILKIIAFGV LNYFRDAWNV FDFVTVLGSI TDILVTEIAN NFINLSFLRL 

      1570       1580       1590       1600       1610       1620 
FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIALDDD 

      1630       1640       1650       1660       1670       1680 
TSINRHNNFR TFLQALMLLF RSATGEAWHE IMLSCLGNRA CDPHANASEC GSDFAYFYFV 

      1690       1700       1710       1720       1730       1740 
SFIFLCSFLM LNLFVAVIMD NFEYLTRDSS ILGPHHLDEF IRVWAEYDPA ACGRISYNDM 

      1750       1760       1770       1780       1790       1800 
FEMLKHMSPP LGLGKKCPAR VAYKRLVRMN MPISNEDMTV HFTSTLMALI RTALEIKLAP 

      1810       1820       1830       1840       1850       1860 
AGTKQHQCDA ELRKEISSVW ANLPQKTLDL LVPPHKPDEM TVGKVYAALM IFDFYKQNKT 

      1870       1880       1890       1900       1910       1920 
TRDQTHQAPG GLSQMGPVSL FHPLKATLEQ TQPAVLRGAR VFLRQKSATS LSNGGAIQTQ 

      1930       1940       1950       1960       1970       1980 
ESGIKESLSW GTQRTQDALY EARAPLERGH SAEIPVGQSG TLAVDVQMQN MTLRGPDGEP 

      1990       2000       2010       2020       2030       2040 
QPGLESQGRA ASMPRLAAET QPAPNASPMK RSISTLAPRP HGTQLCSTVL DRPPPSQASH 

      2050       2060       2070       2080       2090       2100 
HHHHRCHRRR DKKQRSLEKG PSLSVDPEGA PSTAAGPGLP HGEGSTACRR DRKQERGRSQ 

      2110       2120       2130       2140       2150       2160 
ERRQPSSSSS EKQRFYSCDR FGSREPPQLM PSLSSHPTSP TAALEPAPHP QGSGSVNGSP 

      2170       2180       2190       2200       2210       2220 
LMSTSGASTP GRGGRRQLPQ TPLTPRPSIT YKTANSSPVH FAEGQSGLPA FSPGRLSRGL 

      2230       2240       2250       2260       2270       2280 
SEHNALLQKE PLSQPLAPGS RIGSDPYLGQ RLDSEASAHT LPEDTLTFEE AVATNSGRSS 

      2290       2300       2310       2320 
RTSYVSSLTS QSHPLRRVPN GYHCTLGLST GVRARHSYHH PDQDHWC 

« Hide

Isoform NB2 [UniParc].

Checksum: 16B0576EA8DCACC6
Show »

FASTA2,348263,674

References

« Hide 'large scale' references
[1]"Nucleotide sequence polymorphism of mouse alpha1 B."
Hong T., Birnbaumer L.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]"Molecular cloning of a murine N-type calcium channel alpha 1 subunit. Evidence for isoforms, brain distribution, and chromosomal localization."
Coppola T., Waldmann R., Borsotto M., Heurteaux C., Romey G., Mattei M.-G., Lazdunski M.
FEBS Lett. 338:1-5(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NB1 AND NB2).
Tissue: Neuroblastoma.
[3]"Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin."
Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G., Regazzi R.
J. Biol. Chem. 276:32756-32762(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIMS1.
Tissue: Brain.
[4]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF042317 mRNA. Translation: AAB97840.1.
U04999 mRNA. Translation: AAB60437.1. Frameshift.
PIRS41080.
RefSeqNP_001035993.1. NM_001042528.2.
UniGeneMm.4424.

3D structure databases

ProteinModelPortalO55017.
SMRO55017. Positions 97-407, 475-712, 1135-1410, 1466-1865.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198431. 4 interactions.
IntActO55017. 1 interaction.

Protein family/group databases

TCDB1.A.1.11.9. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteO55017.

Proteomic databases

PaxDbO55017.
PRIDEO55017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041342; ENSMUSP00000037416; ENSMUSG00000004113. [O55017-1]
GeneID12287.
KEGGmmu:12287.
UCSCuc008ipe.1. mouse. [O55017-1]

Organism-specific databases

CTD774.
MGIMGI:88296. Cacna1b.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00750000117449.
HOGENOMHOG000231530.
HOVERGENHBG050763.
KOK04849.
TreeFamTF312805.

Gene expression databases

ArrayExpressO55017.
BgeeO55017.
GenevestigatorO55017.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280760.
PROO55017.
SOURCESearch...

Entry information

Entry nameCAC1B_MOUSE
AccessionPrimary (citable) accession number: O55017
Secondary accession number(s): Q60609
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot