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O00555 (CAC1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Alternative name(s):
Brain calcium channel I
Short name=BI
Calcium channel, L type, alpha-1 polypeptide isoform 4
Voltage-gated calcium channel subunit alpha Cav2.1
Gene names
Name:CACNA1A
Synonyms:CACH4, CACN3, CACNL1A4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length2505 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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).

Subunit structure

Voltage-dependent calcium channels are multisubunit complexes, 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. Interact (via C-terminal CDB motif) with CABP1 in the pre- and postsynaptic membranes.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Brain specific; mainly found in cerebellum, cerebral cortex, thalamus and hypothalamus. Expressed in the small cell lung carcinoma cell line SCC-9. No expression in heart, kidney, liver or muscle. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells. Ref.6

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.

Polymorphism

The poly-Gln region of CACNA1A is polymorphic: 6 to 17 repeats in the normal population, expanded to about 21 to 30 repeats in SCA6. Repeat expansion has been reported also in a EA2 family.

Involvement in disease

Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:183086]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder. Ref.3 Ref.10 Ref.11 Ref.24 Ref.29

Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:141500]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy. Ref.2 Ref.13 Ref.14 Ref.16 Ref.20 Ref.25

Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:108500]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy. Ref.2 Ref.11 Ref.12 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.26 Ref.27 Ref.30

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1A subfamily. [View classification]

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O00555-1)

Also known as: 1A-1; BI-1-GGCAG;

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 2 (identifier: O00555-2)

Also known as: 1A-2,BI-1;

The sequence of this isoform differs from the canonical sequence as follows:
     2262-2505: Missing.
Isoform 3 (identifier: O00555-3)

Also known as: BI-1(V1);

The sequence of this isoform differs from the canonical sequence as follows:
     1844-1875: WGRMPYLDMYQMLRHMSPPLGLGKKCPARVAY → CGRIHYKDMYSLLRVISPPLGLGKKCPHRVAC
     2262-2505: Missing.
Isoform 4 (identifier: O00555-4)

Also known as: BI-1(V1)-GGCAG;

The sequence of this isoform differs from the canonical sequence as follows:
     1844-1875: WGRMPYLDMYQMLRHMSPPLGLGKKCPARVAY → CGRIHYKDMYSLLRVISPPLGLGKKCPHRVAC
Isoform 5 (identifier: O00555-5)

Also known as: BI-1(V2);

The sequence of this isoform differs from the canonical sequence as follows:
     2103-2114: Missing.
     2262-2505: Missing.
Isoform 6 (identifier: O00555-6)

Also known as: BI-1(V2)-GGCAG;

The sequence of this isoform differs from the canonical sequence as follows:
     2103-2114: Missing.
Isoform 7 (identifier: O00555-7)

Also known as: BI-1(V2,V3);

The sequence of this isoform differs from the canonical sequence as follows:
     2220-2240: HPPPPDKDRYAQERPDHGRAR → RFLCFFFPFFLPCLKTVGLGL
     2241-2505: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25052505Voltage-dependent P/Q-type calcium channel subunit alpha-1A
PRO_0000053916

Regions

Topological domain1 – 9898Cytoplasmic Potential
Transmembrane99 – 11719Helical; Name=S1 of repeat I; Potential
Topological domain118 – 13518Extracellular Potential
Transmembrane136 – 15520Helical; Name=S2 of repeat I; Potential
Topological domain156 – 16712Cytoplasmic Potential
Transmembrane168 – 18518Helical; Name=S3 of repeat I; Potential
Topological domain186 – 1905Extracellular Potential
Transmembrane191 – 20919Helical; Name=S4 of repeat I; Potential
Topological domain210 – 22819Cytoplasmic Potential
Transmembrane229 – 24820Helical; Name=S5 of repeat I; Potential
Topological domain249 – 33587Extracellular Potential
Transmembrane336 – 36025Helical; Name=S6 of repeat I; Potential
Topological domain361 – 487127Cytoplasmic Potential
Transmembrane488 – 50619Helical; Name=S1 of repeat II; Potential
Topological domain507 – 52115Extracellular Potential
Transmembrane522 – 54120Helical; Name=S2 of repeat II; Potential
Topological domain542 – 5498Cytoplasmic Potential
Transmembrane550 – 56819Helical; Name=S3 of repeat II; Potential
Topological domain569 – 57810Extracellular Potential
Transmembrane579 – 59719Helical; Name=S4 of repeat II; Potential
Topological domain598 – 61619Cytoplasmic Potential
Transmembrane617 – 63620Helical; Name=S5 of repeat II; Potential
Topological domain637 – 68953Extracellular Potential
Transmembrane690 – 71425Helical; Name=S6 of repeat II; Potential
Topological domain715 – 1242528Cytoplasmic Potential
Transmembrane1243 – 126119Helical; Name=S1 of repeat III; Potential
Topological domain1262 – 127716Extracellular Potential
Transmembrane1278 – 129720Helical; Name=S2 of repeat III; Potential
Topological domain1298 – 130912Cytoplasmic Potential
Transmembrane1310 – 132819Helical; Name=S3 of repeat III; Potential
Topological domain1329 – 133911Extracellular Potential
Transmembrane1340 – 135819Helical; Name=S4 of repeat III; Potential
Topological domain1359 – 137719Cytoplasmic Potential
Transmembrane1378 – 139720Helical; Name=S5 of repeat III; Potential
Topological domain1398 – 148487Extracellular Potential
Transmembrane1485 – 150925Helical; Name=S6 of repeat III; Potential
Topological domain1510 – 156455Cytoplasmic Potential
Transmembrane1565 – 159329Helical; Name=S1 of repeat IV; Potential
Topological domain1594 – 15985Extracellular Potential
Transmembrane1599 – 161820Helical; Name=S2 of repeat IV; Potential
Topological domain1619 – 16268Cytoplasmic Potential
Transmembrane1627 – 164519Helical; Name=S3 of repeat IV; Potential
Topological domain1646 – 16527Extracellular Potential
Transmembrane1653 – 167119Helical; Name=S4 of repeat IV; Potential
Topological domain1672 – 169019Cytoplasmic Potential
Transmembrane1691 – 171020Helical; Name=S5 of repeat IV; Potential
Topological domain1711 – 178272Extracellular Potential
Transmembrane1783 – 180725Helical; Name=S6 of repeat IV; Potential
Topological domain1808 – 2505698Cytoplasmic Potential
Repeat85 – 363279I
Repeat473 – 717245II
Repeat1231 – 1514284III
Repeat1551 – 1814264IV
Calcium binding1840 – 185112 By similarity
Region383 – 40018Binding to the beta subunit By similarity
Compositional bias13 – 186Poly-Gly
Compositional bias727 – 7326Poly-Glu
Compositional bias1002 – 10076Poly-Arg
Compositional bias1204 – 12074Poly-Glu
Compositional bias2211 – 222010Poly-His
Compositional bias2221 – 22244Poly-Pro
Compositional bias2314 – 232411Poly-Gln

Sites

Site3181Calcium ion selectivity and permeability By similarity
Site6681Calcium ion selectivity and permeability By similarity
Site14601Calcium ion selectivity and permeability By similarity
Site16491Binds to omega-Aga-IVA By similarity
Site17561Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue7501Phosphoserine By similarity
Modified residue18221Phosphoserine; by PKA Potential
Modified residue20301Phosphoserine By similarity
Modified residue20761Phosphotyrosine By similarity
Modified residue22691Phosphoserine By similarity
Modified residue23781Phosphoserine By similarity
Glycosylation2831N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1844 – 187532WGRMP…ARVAY → CGRIHYKDMYSLLRVISPPL GLGKKCPHRVAC in isoform 3 and isoform 4.
VSP_000871
Alternative sequence2103 – 211412Missing in isoform 5 and isoform 6.
VSP_000872
Alternative sequence2220 – 224021HPPPP…HGRAR → RFLCFFFPFFLPCLKTVGLG L in isoform 7.
VSP_000873
Alternative sequence2241 – 2505265Missing in isoform 7.
VSP_000874
Alternative sequence2262 – 2505244Missing in isoform 2, isoform 3 and isoform 5.
VSP_000875
Natural variant211A → V.
Corresponds to variant rs15999 [ dbSNP | Ensembl ].
VAR_014456
Natural variant1921R → Q in FHM1. Ref.2
Corresponds to variant rs121908211 [ dbSNP | Ensembl ].
VAR_001491
Natural variant1951R → K in FHM1. Ref.16
Corresponds to variant rs121908222 [ dbSNP | Ensembl ].
VAR_043820
Natural variant2181S → L in FHM1. Ref.14
Corresponds to variant rs121908225 [ dbSNP | Ensembl ].
VAR_043821
Natural variant2481Y → C in EA2. Ref.26
Corresponds to variant rs121908238 [ dbSNP | Ensembl ].
VAR_063683
Natural variant2531H → Y in EA2. Ref.18
Corresponds to variant rs121908228 [ dbSNP | Ensembl ].
VAR_043822
Natural variant2561C → R in EA2. Ref.21
Corresponds to variant rs121908231 [ dbSNP | Ensembl ].
VAR_043823
Natural variant2871C → Y in EA2. Ref.22
Corresponds to variant rs121908236 [ dbSNP | Ensembl ].
VAR_043824
Natural variant2931G → R in EA2 and SCA6. Ref.10 Ref.22
Corresponds to variant rs121908215 [ dbSNP | Ensembl ].
VAR_043825
Natural variant3891L → F in EA2. Ref.30
Corresponds to variant rs121908239 [ dbSNP | Ensembl ].
VAR_063684
Natural variant4051A → T in SCA6. Ref.29
Corresponds to variant rs1219082456 [ dbSNP | Ensembl ].
VAR_063685
Natural variant4541A → T. Ref.2
Corresponds to variant rs41276886 [ dbSNP | Ensembl ].
VAR_063686
Natural variant5011T → M in EA2. Ref.30
Corresponds to variant rs121908240 [ dbSNP | Ensembl ].
VAR_063687
Natural variant5831R → Q in FHM1. Ref.16
Corresponds to variant rs121908217 [ dbSNP | Ensembl ].
VAR_043826
Natural variant6381G → D in EA2; reduces P/Q current densities. Ref.27
Corresponds to variant rs121908246 [ dbSNP | Ensembl ].
VAR_063688
Natural variant6661T → M in FHM1 and EA2. Ref.2 Ref.16 Ref.22
Corresponds to variant rs121908212 [ dbSNP | Ensembl ].
VAR_001492
Natural variant7141V → A in FHM1. Ref.2
Corresponds to variant rs121908213 [ dbSNP | Ensembl ].
VAR_001493
Natural variant7151D → E in FHM1. Ref.16
Corresponds to variant rs121908218 [ dbSNP | Ensembl ].
VAR_043827
Natural variant7321E → A.
Corresponds to variant rs16019 [ dbSNP | Ensembl ].
VAR_059221
Natural variant7981M → T in EA2. Ref.30
Corresponds to variant rs121908241 [ dbSNP | Ensembl ].
VAR_063689
Natural variant8971P → R in EA2. Ref.30
Corresponds to variant rs121908242 [ dbSNP | Ensembl ].
VAR_063690
Natural variant9141P → S.
Corresponds to variant rs16020 [ dbSNP | Ensembl ].
VAR_014458
Natural variant9181E → D. Ref.23 Ref.28
Corresponds to variant rs16022 [ dbSNP | Ensembl ].
VAR_014459
Natural variant9931E → V. Ref.13 Ref.23 Ref.28
Corresponds to variant rs16023 [ dbSNP | Ensembl ].
VAR_043828
Natural variant10151E → K.
Corresponds to variant rs16024 [ dbSNP | Ensembl ].
VAR_014461
Natural variant11051G → S. Ref.23
Corresponds to variant rs16027 [ dbSNP | Ensembl ].
VAR_014462
Natural variant11731P → L.
Corresponds to variant rs16028 [ dbSNP | Ensembl ].
VAR_059222
Natural variant13351K → E in FHM1. Ref.16
Corresponds to variant rs121908223 [ dbSNP | Ensembl ].
VAR_043829
Natural variant13461R → Q in FHM1; with progressive cerebellar ataxia. Ref.20 Ref.25
Corresponds to variant rs121908230 [ dbSNP | Ensembl ].
VAR_043830
Natural variant13841Y → C in FHM1. Ref.16
Corresponds to variant rs121908219 [ dbSNP | Ensembl ].
VAR_043831
Natural variant14031F → C in EA2; loss of function. Ref.17
Corresponds to variant rs121908227 [ dbSNP | Ensembl ].
VAR_043832
Natural variant14561V → L in FHM1. Ref.13
Corresponds to variant rs121908237 [ dbSNP | Ensembl ].
VAR_043833
Natural variant14821G → R in EA2. Ref.21
Corresponds to variant rs121908232 [ dbSNP | Ensembl ].
VAR_043834
Natural variant14901F → S in EA2. Ref.21
Corresponds to variant rs121908233 [ dbSNP | Ensembl ].
VAR_043835
Natural variant14931V → I in EA2. Ref.21
Corresponds to variant rs121908234 [ dbSNP | Ensembl ].
VAR_043836
Natural variant16611R → H in EA2. Ref.12
Corresponds to variant rs121908216 [ dbSNP | Ensembl ].
VAR_043837
Natural variant16641R → Q in SCA6. Ref.24
Corresponds to variant rs121908247 [ dbSNP | Ensembl ].
VAR_063691
Natural variant16671R → W in FHM1. Ref.16
Corresponds to variant rs121908220 [ dbSNP | Ensembl ].
VAR_043838
Natural variant16791R → C in EA2. Ref.30
Corresponds to variant rs121908243 [ dbSNP | Ensembl ].
VAR_063692
Natural variant16831W → R in FHM1. Ref.16
Corresponds to variant rs121908221 [ dbSNP | Ensembl ].
VAR_043839
Natural variant16951V → I in FHM1. Ref.16
Corresponds to variant rs121908224 [ dbSNP | Ensembl ].
VAR_063706
Natural variant17361H → L in EA2. Ref.19
Corresponds to variant rs121908229 [ dbSNP | Ensembl ].
VAR_043840
Natural variant17561E → K in EA2. Ref.15
Corresponds to variant rs121908226 [ dbSNP | Ensembl ].
VAR_043841
Natural variant18101I → L in FHM1. Ref.2
Corresponds to variant rs121908214 [ dbSNP | Ensembl ].
VAR_001494
Natural variant18691C → R in EA2. Ref.30
Corresponds to variant rs121908244 [ dbSNP | Ensembl ].
VAR_063693
Natural variant21351R → C in EA2. Ref.21
Corresponds to variant rs121908235 [ dbSNP | Ensembl ].
VAR_043842
Natural variant23941P → S.
Corresponds to variant rs16056 [ dbSNP | Ensembl ].
VAR_014463

Experimental info

Sequence conflict7251K → KVEA in AAB61613. Ref.1
Sequence conflict7251K → KVEA in AAB61612. Ref.1
Sequence conflict8961G → D in CAA68172. Ref.2
Sequence conflict12071E → EE in CAA68172. Ref.2
Sequence conflict1313 – 13153WNI → ILP in AAB49674. Ref.3
Sequence conflict1313 – 13153WNI → ILP in AAB49675. Ref.3
Sequence conflict1313 – 13153WNI → ILP in AAB49676. Ref.3
Sequence conflict1313 – 13153WNI → ILP in AAB49677. Ref.3
Sequence conflict1313 – 13153WNI → ILP in AAB49678. Ref.3
Sequence conflict14591G → A in CAA68172. Ref.2
Sequence conflict16041V → A in CAA68172. Ref.2
Sequence conflict16171V → A in CAA68172. Ref.2
Sequence conflict16511G → GNP in AAB61613. Ref.1
Sequence conflict16511G → GNP in AAB61612. Ref.1
Sequence conflict16931P → A in AAB33068. Ref.5
Sequence conflict20381E → G in U06702. Ref.7
Sequence conflict23141Q → QQ in AAB49676. Ref.3

Secondary structure

1 ... 2505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (1A-1) (BI-1-GGCAG) [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 2F2F378ACE02FD56

FASTA2,505282,365
        10         20         30         40         50         60 
MARFGDEMPA RYGGGGSGAA AGVVVGSGGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA 

        70         80         90        100        110        120 
LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH 

       130        140        150        160        170        180 
LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG 

       190        200        210        220        230        240 
ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF 

       250        260        270        280        290        300 
AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTKCQPY WEGPNNGITQ 

       310        320        330        340        350        360 
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS 

       370        380        390        400        410        420 
GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD GEQRHPFDGA 

       430        440        450        460        470        480 
LRRTTIKKSK TDLLNPEEAE DQLADIASVG SPFARASIKS AKLENSTFFH KKERRMRFYI 

       490        500        510        520        530        540 
RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG 

       550        560        570        580        590        600 
LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL 

       610        620        630        640        650        660 
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT 

       670        680        690        700        710        720 
VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA 

       730        740        750        760        770        780 
QELTKDEQEE EEAANQKLAL QKAKEVAEVS PLSAANMSIA VKEQQKNQKP AKSVWEQRTS 

       790        800        810        820        830        840 
EMRKQNLLAS REALYNEMDP DERWKAAYTR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR 

       850        860        870        880        890        900 
AAEPTVDQRL GQQRAEDFLR KQARYHDRAR DPSGSAGLDA RRPWAGSQEA ELSREGPYGR 

       910        920        930        940        950        960 
ESDHHAREGS LEQPGFWEGE AERGKAGDPH RRHVHRQGGS RESRSGSPRT GADGEHRRHR 

       970        980        990       1000       1010       1020 
AHRRPGEEGP EDKAERRARH REGSRPARGG EGEGEGPDGG ERRRRHRHGA PATYEGDARR 

      1030       1040       1050       1060       1070       1080 
EDKERRHRRR KENQGSGVPV SGPNLSTTRP IQQDLGRQDP PLAEDIDNMK NNKLATAESA 

      1090       1100       1110       1120       1130       1140 
APHGSLGHAG LPQSPAKMGN STDPGPMLAI PAMATNPQNA ASRRTPNNPG NPSNPGPPKT 

      1150       1160       1170       1180       1190       1200 
PENSLIVTNP SGTQTNSAKT ARKPDHTTVD IPPACPPPLN HTVVQVNKNA NPDPLPKKEE 

      1210       1220       1230       1240       1250       1260 
EKKEEEEDDR GEDGPKPMPP YSSMFILSTT NPLRRLCHYI LNLRYFEMCI LMVIAMSSIA 

      1270       1280       1290       1300       1310       1320 
LAAEDPVQPN APRNNVLRYF DYVFTGVFTF EMVIKMIDLG LVLHQGAYFR DLWNILDFIV 

      1330       1340       1350       1360       1370       1380 
VSGALVAFAF TGNSKGKDIN TIKSLRVLRV LRPLKTIKRL PKLKAVFDCV VNSLKNVFNI 

      1390       1400       1410       1420       1430       1440 
LIVYMLFMFI FAVVAVQLFK GKFFHCTDES KEFEKDCRGK YLLYEKNEVK ARDREWKKYE 

      1450       1460       1470       1480       1490       1500 
FHYDNVLWAL LTLFTVSTGE GWPQVLKHSV DATFENQGPS PGYRMEMSIF YVVYFVVFPF 

      1510       1520       1530       1540       1550       1560 
FFVNIFVALI IITFQEQGDK MMEEYSLEKN ERACIDFAIS AKPLTRHMPQ NKQSFQYRMW 

      1570       1580       1590       1600       1610       1620 
QFVVSPPFEY TIMAMIALNT IVLMMKFYGA SVAYENALRV FNIVFTSLFS LECVLKVMAF 

      1630       1640       1650       1660       1670       1680 
GILNYFRDAW NIFDFVTVLG SITDILVTEF GNNFINLSFL RLFRAARLIK LLRQGYTIRI 

      1690       1700       1710       1720       1730       1740 
LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG MQVFGNIGID VEDEDSDEDE FQITEHNNFR 

      1750       1760       1770       1780       1790       1800 
TFFQALMLLF RSATGEAWHN IMLSCLSGKP CDKNSGILTR ECGNEFAYFY FVSFIFLCSF 

      1810       1820       1830       1840       1850       1860 
LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EYVRVWAEYD PAAWGRMPYL DMYQMLRHMS 

      1870       1880       1890       1900       1910       1920 
PPLGLGKKCP ARVAYKRLLR MDLPVADDNT VHFNSTLMAL IRTALDIKIA KGGADKQQMD 

      1930       1940       1950       1960       1970       1980 
AELRKEMMAI WPNLSQKTLD LLVTPHKSTD LTVGKIYAAM MIMEYYRQSK AKKLQAMREE 

      1990       2000       2010       2020       2030       2040 
QDRTPLMFQR MEPPSPTQEG GPGQNALPST QLDPGGALMA HESGLKESPS WVTQRAQEMF 

      2050       2060       2070       2080       2090       2100 
QKTGTWSPEQ GPPTDMPNSQ PNSQSVEMRE MGRDGYSDSE HYLPMEGQGR AASMPRLPAE 

      2110       2120       2130       2140       2150       2160 
NQRRRGRPRG NNLSTISDTS PMKRSASVLG PKARRLDDYS LERVPPEENQ RHHQRRRDRS 

      2170       2180       2190       2200       2210       2220 
HRASERSLGR YTDVDTGLGT DLSMTTQSGD LPSKERDQER GRPKDRKHRQ HHHHHHHHHH 

      2230       2240       2250       2260       2270       2280 
PPPPDKDRYA QERPDHGRAR ARDQRWSRSP SEGREHMAHR QGSSSVSGSP APSTSGTSTP 

      2290       2300       2310       2320       2330       2340 
RRGRRQLPQT PSTPRPHVSY SPVIRKAGGS GPPQQQQQQQ QQQQAVARPG RAATSGPRRY 

      2350       2360       2370       2380       2390       2400 
PGPTAEPLAG DRPPTGGHSS GRSPRMERRV PGPARSESPR ACRHGGARWP ASGPHVSEGP 

      2410       2420       2430       2440       2450       2460 
PGPRHHGYYR GSDYDEADGP GSGGGEEAMA GAYDAPPPVR HASSGATGRS PRTPRASGPA 

      2470       2480       2490       2500 
CASPSRHGRR LPNGYYPAHG LARPRGPGSR KGLHEPYSES DDDWC

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Isoform 2 (1A-2,BI-1) [UniParc].

Checksum: 08A864BB400F218B
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FASTA2,261256,932
Isoform 3 (BI-1(V1)) [UniParc].

Checksum: 41408D8C7EB70094
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FASTA2,261256,777
Isoform 4 (BI-1(V1)-GGCAG) [UniParc].

Checksum: ED4AA00D118EF46B
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FASTA2,505282,209
Isoform 5 (BI-1(V2)) [UniParc].

Checksum: 729D79965A9714A4
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FASTA2,249255,511
Isoform 6 (BI-1(V2)-GGCAG) [UniParc].

Checksum: 212024798B9867E3
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FASTA2,493280,944
Isoform 7 (BI-1(V2,V3)) [UniParc].

Checksum: 3E9FDBB527ED3E46
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FASTA2,240254,343

References

« Hide 'large scale' references
[1]"Structural elements in domain IV that influence biophysical and pharmacological properties of human alpha1A-containing high-voltage-activated calcium channels."
Hans M., Urrutia A., Deal C., Brust P.F., Stauderman K., Ellis S.B., Harpold M.M., Johnson E.C., Williams M.E.
Biophys. J. 76:1384-1400(1999) [PubMed: 10049321] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Neuron.
[2]"Familial hemiplegic migraine and episodic ataxia type-2 are caused by mutations in the Ca2+ channel gene CACNL1A4."
Ophoff R.A., Terwindt G.M., Vergouwe M.N., van Eijk R., Oefner P.J., Hoffman S.M.G., Lamerdin J.E., Mohrenweiser H.W., Bulman D.E., Ferrari M., Haan J., Lindhout D., van Ommen G.-J.B., Hofker M.H., Ferrari M.D., Frants R.R.
Cell 87:543-552(1996) [PubMed: 8898206] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), VARIANTS FHM1 GLN-192; MET-666; ALA-714 AND LEU-1810, VARIANT THR-454, INVOLVEMENT IN EA2.
Tissue: Cerebellum.
[3]"Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel."
Zhuchenko O., Bailey J., Bonnen P.E., Ashizawa T., Stockton D.W., Amos C., Dobyns W.B., Subramony S.H., Zoghbi H.Y., Lee C.C.
Nat. Genet. 15:62-69(1997) [PubMed: 8988170] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 1313-2505 (ISOFORMS 1; 2; 3; 6 AND 7), ALTERNATIVE SPLICING, INVOLVEMENT IN SCA6.
Tissue: Brain.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Expression and antibody inhibition of P-type calcium channels in human small-cell lung carcinoma cells."
Barry E.L.R., Viglione M.P., Kim Y.I., Froehner S.C.
J. Neurosci. 15:274-283(1995) [PubMed: 7823133] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1693-1807.
Tissue: Lung carcinoma.
[6]"Molecular diversity of neuronal-type calcium channels identified in small cell lung carcinoma."
Oguro-Okano M., Griesmann G.E., Wieben E.D., Slaymaker S.J., Snutch T.P., Lennon V.A.
Mayo Clin. Proc. 67:1150-1159(1992) [PubMed: 1335101] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1702-1822, TISSUE SPECIFICITY.
Tissue: Lung carcinoma.
[7]"Characterization of cDNA clones containing CCA trinucleotide repeats derived from human brain."
Margolis R.L., Breschel T.S., Li S.H., Kidwai A.S., Antonarakis S.E., McInnis M.G., Ross C.A.
Somat. Cell Mol. Genet. 21:279-284(1995) [PubMed: 8525433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2038-2258 (ISOFORMS 1/2/3/4).
Tissue: Frontal cortex.
[8]"Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1."
Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T., Catterall W.A.
Nat. Neurosci. 5:210-217(2002) [PubMed: 11865310] [Abstract]
Cited for: INTERACTION WITH CABP1.
[9]"Crystal structure of the CaV2 IQ domain in complex with Ca2+/calmodulin: high-resolution mechanistic implications for channel regulation by Ca2+."
Mori M.X., Vander Kooi C.W., Leahy D.J., Yue D.T.
Structure 16:607-620(2008) [PubMed: 18400181] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1955-1975.
[10]"Progressive ataxia due to a missense mutation in a calcium-channel gene."
Yue Q., Jen J.C., Nelson S.F., Baloh R.W.
Am. J. Hum. Genet. 61:1078-1087(1997) [PubMed: 9345107] [Abstract]
Cited for: VARIANT SCA6 ARG-293.
[11]"Episodic ataxia type 2 (EA2) and spinocerebellar ataxia type 6 (SCA6) due to CAG repeat expansion in the CACNA1A gene on chromosome 19p."
Jodice C., Mantuano E., Veneziano L., Trettel F., Sabbadini G., Calandriello L., Francia A., Spadaro M., Pierelli F., Salvi F., Ophoff R.A., Frants R.R., Frontali M.
Hum. Mol. Genet. 6:1973-1978(1997) [PubMed: 9302278] [Abstract]
Cited for: POLYMORPHISM, INVOLVEMENT IN SCA6 AND EA2.
[12]"Detection of a novel missense mutation and second recurrent mutation in the CACNA1A gene in individuals with EA-2 and FHM."
Friend K.L., Crimmins D., Phan T.G., Sue C.M., Colley A., Fung V.S., Morris J.G., Sutherland G.R., Richards R.I.
Hum. Genet. 105:261-265(1999) [PubMed: 10987655] [Abstract]
Cited for: VARIANT EA2 HIS-1661.
[13]"Genetic heterogeneity in Italian families with familial hemiplegic migraine."
Carrera P., Piatti M., Stenirri S., Grimaldi L.M., Marchioni E., Curcio M., Righetti P.G., Ferrari M., Gelfi C.
Neurology 53:26-33(1999) [PubMed: 10408532] [Abstract]
Cited for: VARIANT VAL-993, VARIANT FHM1 LEU-1456.
[14]"Delayed cerebral edema and fatal coma after minor head trauma: role of the CACNA1A calcium channel subunit gene and relationship with familial hemiplegic migraine."
Kors E.E., Terwindt G.M., Vermeulen F.L., Fitzsimons R.B., Jardine P.E., Heywood P., Love S., van den Maagdenberg A.M., Haan J., Frants R.R., Ferrari M.D.
Ann. Neurol. 49:753-760(2001) [PubMed: 11409427] [Abstract]
Cited for: VARIANT FHM1 LEU-218.
[15]"Missense CACNA1A mutation causing episodic ataxia type 2."
Denier C., Ducros A., Durr A., Eymard B., Chassande B., Tournier-Lasserve E.
Arch. Neurol. 58:292-295(2001) [PubMed: 11176968] [Abstract]
Cited for: VARIANT EA2 LYS-1756.
[16]"The clinical spectrum of familial hemiplegic migraine associated with mutations in a neuronal calcium channel."
Ducros A., Denier C., Joutel A., Cecillon M., Lescoat C., Vahedi K., Darcel F., Vicaut E., Bousser M.G., Tournier-Lasserve E.
N. Engl. J. Med. 345:17-24(2001) [PubMed: 11439943] [Abstract]
Cited for: VARIANTS FHM1 LYS-195; GLN-583; MET-666; GLU-715; GLU-1335; CYS-1384; TRP-1667; ARG-1683 AND ILE-1695.
[17]"Loss-of-function EA2 mutations are associated with impaired neuromuscular transmission."
Jen J., Wan J., Graves M., Yu H., Mock A.F., Coulin C.J., Kim G., Yue Q., Papazian D.M., Baloh R.W.
Neurology 57:1843-1848(2001) [PubMed: 11723274] [Abstract]
Cited for: VARIANT EA2 CYS-1403, CHARACTERIZATION OF VARIANT EA2 CYS-1403.
[18]"Episodic ataxia type 2. Three novel truncating mutations and one novel missense mutation in the CACNA1A gene."
van den Maagdenberg A.M., Kors E.E., Brunt E.R., van Paesschen W., Pascual J., Ravine D., Keeling S., Vanmolkot K.R., Vermeulen F.L., Terwindt G.M., Haan J., Frants R.R., Ferrari M.D.
J. Neurol. 249:1515-1519(2002) [PubMed: 12420090] [Abstract]
Cited for: VARIANT EA2 TYR-253.
[19]"Functional implications of a novel EA2 mutation in the P/Q-type calcium channel."
Spacey S.D., Hildebrand M.E., Materek L.A., Bird T.D., Snutch T.P.
Ann. Neurol. 56:213-220(2004) [PubMed: 15293273] [Abstract]
Cited for: VARIANT EA2 LEU-1736.
[20]"A novel R1347Q mutation in the predicted voltage sensor segment of the P/Q-type calcium-channel alpha-subunit in a family with progressive cerebellar ataxia and hemiplegic migraine."
Alonso I., Barros J., Tuna A., Seixas A., Coutinho P., Sequeiros J., Silveira I.
Clin. Genet. 65:70-72(2004) [PubMed: 15032980] [Abstract]
Cited for: VARIANT FHM1 GLN-1346.
[21]"Clusters of non-truncating mutations of P/Q type Ca2+ channel subunit Ca(v)2.1 causing episodic ataxia 2."
Mantuano E., Veneziano L., Spadaro M., Giunti P., Guida S., Leggio M.G., Verriello L., Wood N., Jodice C., Frontali M.
J. Med. Genet. 41:E82-E82(2004) [PubMed: 15173248] [Abstract]
Cited for: VARIANTS EA2 ARG-256; ARG-1482; SER-1490; ILE-1493 AND CYS-2135.
[22]"Clinical spectrum of episodic ataxia type 2."
Jen J., Kim G.W., Baloh R.W.
Neurology 62:17-22(2004) [PubMed: 14718690] [Abstract]
Cited for: VARIANTS EA2 TYR-287; ARG-293 AND MET-666.
[23]"Migrainous vertigo: mutation analysis of the candidate genes CACNA1A, ATP1A2, SCN1A, and CACNB4."
von Brevern M., Ta N., Shankar A., Wiste A., Siegel A., Radtke A., Sander T., Escayg A.
Headache 46:1136-1141(2006) [PubMed: 16866717] [Abstract]
Cited for: VARIANTS ASP-918; VAL-993 AND SER-1105.
[24]"Early onset, non fluctuating spinocerebellar ataxia and a novel missense mutation in CACNA1A gene."
Tonelli A., D'Angelo M.G., Salati R., Villa L., Germinasi C., Frattini T., Meola G., Turconi A.C., Bresolin N., Bassi M.T.
J. Neurol. Sci. 241:13-17(2006) [PubMed: 16325861] [Abstract]
Cited for: VARIANT SCA6 GLN-1664.
[25]"CACNA1A R1347Q: a frequent recurrent mutation in hemiplegic migraine."
Stam A.H., Vanmolkot K.R., Kremer H.P., Gartner J., Brown J., Leshinsky-Silver E., Gilad R., Kors E.E., Frankhuizen W.S., Ginjaar H.B., Haan J., Frants R.R., Ferrari M.D., van den Maagdenberg A.M., Terwindt G.M.
Clin. Genet. 74:481-485(2008) [PubMed: 18400034] [Abstract]
Cited for: VARIANT FHM1 GLN-1346.
[26]"Episodic ataxia type 2 showing ictal hyperhidrosis with hypothermia and interictal chronic diarrhea due to a novel CACNA1A mutation."
Zafeiriou D.I., Lehmann-Horn F., Vargiami E., Teflioudi E., Ververi A., Jurkat-Rott K.
Eur. J. Paediatr. Neurol. 13:191-193(2009) [PubMed: 18602318] [Abstract]
Cited for: VARIANT EA2 CYS-248.
[27]"Late-onset episodic ataxia type 2 associated with a novel loss-of-function mutation in the CACNA1A gene."
Cuenca-Leon E., Banchs I., Serra S.A., Latorre P., Fernandez-Castillo N., Corominas R., Valverde M.A., Volpini V., Fernandez-Fernandez J.M., Macaya A., Cormand B.
J. Neurol. Sci. 280:10-14(2009) [PubMed: 19232643] [Abstract]
Cited for: VARIANT EA2 ASP-638, CHARACTERIZATION OF VARIANT EA2 ASP-638.
[28]"The interplay of two single nucleotide polymorphisms in the CACNA1A gene may contribute to migraine susceptibility."
D'Onofrio M., Ambrosini A., Di Mambro A., Arisi I., Santorelli F.M., Grieco G.S., Nicoletti F., Nappi G., Pierelli F., Schoenen J., Buzzi M.G.
Neurosci. Lett. 453:12-15(2009) [PubMed: 19429006] [Abstract]
Cited for: VARIANTS ASP-918 AND VAL-993.
[29]"A wide spectrum of clinical, neurophysiological and neuroradiological abnormalities in a family with a novel CACNA1A mutation."
Romaniello R., Zucca C., Tonelli A., Bonato S., Baschirotto C., Zanotta N., Epifanio R., Righini A., Bresolin N., Bassi M.T., Borgatti R.
J. Neurol. Neurosurg. Psych. 81:840-843(2010) [PubMed: 20682717] [Abstract]
Cited for: VARIANT SCA6 THR-405.
[30]"Identification of novel and recurrent CACNA1A gene mutations in fifteen patients with episodic ataxia type 2."
Mantuano E., Romano S., Veneziano L., Gellera C., Castellotti B., Caimi S., Testa D., Estienne M., Zorzi G., Bugiani M., Rajabally Y.A., Barcina M.J., Servidei S., Panico A., Frontali M., Mariotti C.
J. Neurol. Sci. 291:30-36(2010) [PubMed: 20129625] [Abstract]
Cited for: VARIANTS EA2 PHE-389; MET-501; THR-798; ARG-897; CYS-1679 AND ARG-1869.
+Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF004883 mRNA. Translation: AAB61612.1.
AF004884 mRNA. Translation: AAB61613.1.
X99897 mRNA. Translation: CAA68172.1.
Z80114 Genomic DNA. No translation available.
Z80115 Genomic DNA. No translation available.
U79663 mRNA. Translation: AAB49674.1.
U79664 mRNA. Translation: AAB49675.1.
U79665 mRNA. Translation: AAB49676.1.
U79666 mRNA. Translation: AAB64179.1.
U79667 mRNA. Translation: AAB49677.1.
U79668 mRNA. Translation: AAB49678.1.
AC005305 Genomic DNA. Translation: AAC26839.1.
AC008540 Genomic DNA. No translation available.
AC011446 Genomic DNA. No translation available.
AC022436 Genomic DNA. No translation available.
AC026805 Genomic DNA. No translation available.
AC098781 Genomic DNA. No translation available.
AC124224 Genomic DNA. No translation available.
S76537 mRNA. Translation: AAB33068.1.
U06702 mRNA. No translation available.
IPIIPI00012136.
IPI00217497.
IPI00217498.
IPI00217499.
IPI00291347.
IPI00397553.
IPI00397554.
RefSeqNP_001120693.1. NM_001127221.1.
NP_001120694.1. NM_001127222.1.
NP_001167551.1. NM_001174080.1.
UniGeneHs.501632.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BXKX-ray2.55B/D1955-1975[»]
ProteinModelPortalO00555.
SMRO00555. Positions 475-716, 1555-1972.
ModBaseSearch...

Protein-protein interaction databases

IntActO00555. 2 interactions.
STRINGO00555.

PTM databases

PhosphoSiteO00555.

Proteomic databases

PRIDEO00555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360228; ENSP00000353362; ENSG00000141837.
GeneID773.
KEGGhsa:773.
UCSCuc002mwy.2. human.
uc010dzc.1. human.
uc010dze.1. human.

Organism-specific databases

CTD773.
GeneCardsGC19M013317.
HGNCHGNC:1388. CACNA1A.
MIM108500. phenotype.
141500. phenotype.
183086. phenotype.
601011. gene.
neXtProtNX_O00555.
Orphanet2131. Alternating hemiplegia of childhood.
71518. Benign paroxysmal torticollis of infancy.
569. Familial or sporadic hemiplegic migraine.
97. Familial paroxysmal ataxia.
98758. Spinocerebellar ataxia type 6.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19834.
HOVERGENHBG050763.
InParanoidO00555.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressO00555.
BgeeO00555.
GenevestigatorO00555.
GermOnlineENSG00000141837. Homo sapiens.

Family and domain databases

InterProIPR005821. Ion_trans.
IPR014873. VDCC_a1su_IQ.
IPR005448. VDCC_P/Q_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
KOK04344.
PANTHERPTHR10037:SF59. PQVDCCAlpha1. 1 hit.
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01244. Bepridil.
DB00568. Cinnarizine.
DB00836. Loperamide.
DB00401. Nisoldipine.
DB00230. Pregabalin.
NextBio3122.
SOURCESearch...

Entry information

Entry nameCAC1A_HUMAN
AccessionPrimary (citable) accession number: O00555
Secondary accession number(s): P78510 expand/collapse secondary AC list , P78511, Q16290, Q92690, Q99790, Q99791, Q99792, Q99793, Q9UDC4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: January 25, 2012
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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