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P54282

- CAC1A_RAT

UniProt

P54282 - CAC1A_RAT

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Protein

Voltage-dependent P/Q-type calcium channel subunit alpha-1A

Gene

Cacna1a

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

Functioni

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei320 – 3201Calcium ion selectivity and permeabilityBy similarity
Sitei670 – 6701Calcium ion selectivity and permeabilityBy similarity
Sitei1411 – 14111Calcium ion selectivity and permeabilityBy similarity
Sitei1600 – 16001Binds to omega-Aga-IVABy similarity
Sitei1707 – 17071Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1791 – 180212By similarityAdd
BLAST

GO - Molecular functioni

  1. calmodulin binding Source: UniProtKB
  2. high voltage-gated calcium channel activity Source: RGD
  3. metal ion binding Source: UniProtKB-KW
  4. voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  1. calcium ion import Source: RGD
  2. calcium ion transport Source: RGD
  3. membrane depolarization during action potential Source: RefGenome
  4. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  5. sensory perception of pain Source: RGD
  6. synaptic transmission Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

TCDBi1.A.1.11.8. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended 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
Rat brain class A
Short name:
RBA-I
Voltage-gated calcium channel subunit alpha Cav2.1
Gene namesi
Name:Cacna1a
Synonyms:Cach4, Cacn3, Cacnl1a4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2244. Cacna1a.

Subcellular locationi

GO - Cellular componenti

  1. perikaryon Source: RGD
  2. plasma membrane Source: RGD
  3. protein complex Source: RGD
  4. voltage-gated calcium channel complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22122212Voltage-dependent P/Q-type calcium channel subunit alpha-1APRO_0000053919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Modified residuei792 – 7921PhosphoserineBy similarity
Glycosylationi1607 – 16071N-linked (GlcNAc...)Sequence Analysis
Modified residuei1773 – 17731Phosphoserine; by PKASequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP54282.
PRIDEiP54282.

PTM databases

PhosphoSiteiP54282.

Expressioni

Tissue specificityi

Brain specific. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells. Also found in heart, in kidney distal convoluted tubule (DCT), and in pituitary.

Gene expression databases

GenevestigatoriP54282.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
Rims1Q9JIR44EBI-3507416,EBI-3507436

Protein-protein interaction databases

DIPiDIP-29638N.
IntActiP54282. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP54282.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 100100CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini120 – 13819ExtracellularSequence AnalysisAdd
BLAST
Topological domaini157 – 16812CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini185 – 1928ExtracellularSequence Analysis
Topological domaini212 – 23019CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini251 – 33787ExtracellularSequence AnalysisAdd
BLAST
Topological domaini363 – 489127CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini510 – 52314ExtracellularSequence AnalysisAdd
BLAST
Topological domaini544 – 5518CytoplasmicSequence Analysis
Topological domaini571 – 58010ExtracellularSequence Analysis
Topological domaini600 – 61819CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini639 – 69153ExtracellularSequence AnalysisAdd
BLAST
Topological domaini717 – 1190474CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1215 – 123117ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1252 – 12587CytoplasmicSequence Analysis
Topological domaini1283 – 129311ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1312 – 133019CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1351 – 143787ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1463 – 151856CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1538 – 155114ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1574 – 15807CytoplasmicSequence Analysis
Topological domaini1601 – 16077ExtracellularSequence Analysis
Topological domaini1627 – 164519CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1666 – 173772ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1764 – 2212449CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei101 – 11919Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Transmembranei139 – 15618Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Transmembranei169 – 18416Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Transmembranei193 – 21119Helical; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Transmembranei231 – 25020Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Transmembranei338 – 36225Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Transmembranei490 – 50920Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Transmembranei524 – 54320Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Transmembranei552 – 57019Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Transmembranei581 – 59919Helical; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Transmembranei619 – 63820Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Transmembranei692 – 71625Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Transmembranei1191 – 121424Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1232 – 125120Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1259 – 128224Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1294 – 131118Helical; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1331 – 135020Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1438 – 146225Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1519 – 153719Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1552 – 157322Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1581 – 160020Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1608 – 162619Helical; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1646 – 166520Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1738 – 176326Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati87 – 365279IAdd
BLAST
Repeati475 – 719245IIAdd
BLAST
Repeati1182 – 1465284IIIAdd
BLAST
Repeati1502 – 1765264IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni385 – 40218Binding to the beta subunitBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 208Poly-Gly
Compositional biasi729 – 7346Poly-Glu
Compositional biasi1155 – 11584Poly-Glu
Compositional biasi2162 – 217110Poly-His

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiP54282.
KOiK04344.
PhylomeDBiP54282.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005448. VDCC_P/Q_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF59. PTHR10037:SF59. 1 hit.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P54282-1) [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
MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY
60 70 80 90 100
KQSMAQRART MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP
110 120 130 140 150
PFEYMILATI IANCIVLALE QHLPDDDKTP MSERLDDTEP YFIGIFCFEA
160 170 180 190 200
GIKIVALGFA FHKGSYLRNG WNVMDFVVVL TGILATVGTE FDLRTLRAVR
210 220 230 240 250
VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL IFAIIGLEFY
260 270 280 290 300
MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
310 320 330 340 350
TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS
360 370 380 390 400
FFMLNLVLGV LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK
410 420 430 440 450
AEEVILAEDE TDVEQRHPFD GALRRATLKK SKTDLLNPEE AEDQLADIAS
460 470 480 490 500
VGSPFARASI KSAKLENSTF FHKKERRMRF YIRRMVKTQA FYWTVLSLVA
510 520 530 540 550
LNTLWLAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM YGLGTRPYFH
560 570 580 590 600
SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
610 620 630 640 650
SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP
660 670 680 690 700
TNFDTFPAAI MTVFQILTGE DWNEVMYDEI KSQGGVQGGM VFSIYFIVLT
710 720 730 740 750
LFGNYTLLNV FLAIAVDNLA NAQELTKDEQ EEEEAANQKL ALQKAKEVAE
760 770 780 790 800
VSPLSAANMS IAVKEQQKNQ KPAKSVWEQR TSEMRKQNLL ASREALYGDA
810 820 830 840 850
AERWPTTYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR APEALRQTAR
860 870 880 890 900
PRESARDPDA RRAWPSSPER APGREGPYGR ESEPQQREHA PPREHVPWDA
910 920 930 940 950
DPERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA
960 970 980 990 1000
TRPARAADGE GDDGERKRRH RHGPPAHDDR ERRHRRRKES QGSGVPMSGP
1010 1020 1030 1040 1050
NLSTTRPIQQ DLGRQDLPLA EDLDNMKNNK LATGEPASPH DSLGHSGLPP
1060 1070 1080 1090 1100
SPAKIGNSTN PGPALATNPQ NAASRRTPNN PGNPSNPGPP KTPENSLIVT
1110 1120 1130 1140 1150
NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN ANPDPLPKKE
1160 1170 1180 1190 1200
EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
1210 1220 1230 1240 1250
ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL
1260 1270 1280 1290 1300
GLVLHQGAYF RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR
1310 1320 1330 1340 1350
VLRPLKTIKR LPKLKAVFDC VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF
1360 1370 1380 1390 1400
KGKFFHCTDE SKEFERDCRG KYLLYEKNEV KARDREWKKY DFHYDNVLWA
1410 1420 1430 1440 1450
LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI FYVVYFVVFP
1460 1470 1480 1490 1500
FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
1510 1520 1530 1540 1550
QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR
1560 1570 1580 1590 1600
VFNIVFTSLF SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE
1610 1620 1630 1640 1650
FGNNFINLSF LRLFRAARLI KLLRQGYTIR ILLWTFVQSF KALPYVCLLI
1660 1670 1680 1690 1700
AMLFFIYAII GMQVFGNIGI DGEDEDSDED EFQITEHNNF RTFFQALMLL
1710 1720 1730 1740 1750
FRSATGEAWH NIMLSCLSGK PCDKNSGIQK PECGNEFAYF YFVSFIFLCS
1760 1770 1780 1790 1800
FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
1810 1820 1830 1840 1850
KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA
1860 1870 1880 1890 1900
LIRTALDIKI AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST
1910 1920 1930 1940 1950
DLTVGKIYAA MMIMEYYRQS KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE
1960 1970 1980 1990 2000
GGPSQNALPS TQLDPGGGLM AQESSMKESP SWVTQRAQEM FQKTGTWSPE
2010 2020 2030 2040 2050
RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT RAASMPRLPA
2060 2070 2080 2090 2100
ENQRRRGRPR GNNLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
2110 2120 2130 2140 2150
QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD
2160 2170 2180 2190 2200
RGRPKDRKHR PHHHHHHHHH HPPAPDRERY AQERPDTGRA RAREQRWSRS
2210
PSEGREHATH RQ
Length:2,212
Mass (Da):251,527
Last modified:October 1, 1996 - v1
Checksum:iDFBD7A0F553AFA52
GO
Isoform 2 (identifier: P54282-2) [UniParc]FASTAAdd to Basket

Also known as: RKC8

The sequence of this isoform differs from the canonical sequence as follows:
     1602-1602: G → GNP

Show »
Length:2,214
Mass (Da):251,739
Checksum:iD2ED9869D22AF77F
GO
Isoform 3 (identifier: P54282-3)

Also known as: RBA-65

Sequence is not available
Length:
Mass (Da):
Isoform 4 (identifier: P54282-4)

Sequence is not available
Length:
Mass (Da):

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1602 – 16021G → GNP in isoform 2. 1 PublicationVSP_000881

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64373 mRNA. Translation: AAA40806.1.
M99222 mRNA. Translation: AAA40896.1.
PIRiA41098.
RefSeqiNP_037050.2. NM_012918.3.
UniGeneiRn.87769.

Genome annotation databases

GeneIDi25398.
KEGGirno:25398.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64373 mRNA. Translation: AAA40806.1 .
M99222 mRNA. Translation: AAA40896.1 .
PIRi A41098.
RefSeqi NP_037050.2. NM_012918.3.
UniGenei Rn.87769.

3D structure databases

ProteinModelPortali P54282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29638N.
IntActi P54282. 2 interactions.

Chemistry

BindingDBi P54282.
GuidetoPHARMACOLOGYi 532.

Protein family/group databases

TCDBi 1.A.1.11.8. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei P54282.

Proteomic databases

PaxDbi P54282.
PRIDEi P54282.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25398.
KEGGi rno:25398.

Organism-specific databases

CTDi 773.
RGDi 2244. Cacna1a.

Phylogenomic databases

eggNOGi COG1226.
HOGENOMi HOG000231530.
HOVERGENi HBG050763.
InParanoidi P54282.
KOi K04344.
PhylomeDBi P54282.

Miscellaneous databases

NextBioi 13949997.
PROi P54282.

Gene expression databases

Genevestigatori P54282.

Family and domain databases

Gene3Di 1.20.120.350. 4 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005448. VDCC_P/Q_a1su.
IPR002077. VDCCAlpha1.
[Graphical view ]
PANTHERi PTHR10037:SF59. PTHR10037:SF59. 1 hit.
Pfami PF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view ]
PRINTSi PR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTi SM01062. Ca_chan_IQ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structure of a calcium channel that is highly expressed in the rat cerebellum."
    Starr T.V.B., Prystay W., Snutch T.P.
    Proc. Natl. Acad. Sci. U.S.A. 88:5621-5625(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Molecular characterization and nephron distribution of a family of transcripts encoding the pore-forming subunit of Ca2+ channels in the kidney."
    Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.
    Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1354-1659 (ISOFORM 2).
    Tissue: Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1435-1667 (ISOFORM 3).
  4. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CABP1.

Entry informationi

Entry nameiCAC1A_RAT
AccessioniPrimary (citable) accession number: P54282
Secondary accession number(s): Q01541
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 124 of the entry and version 1 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

External Data

Dasty 3