P11881 · ITPR1_MOUSE

  • Protein
    Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
  • Gene
    Itpr1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Inositol 1,4,5-trisphosphate-gated calcium channel that, upon inositol 1,4,5-trisphosphate binding, mediates calcium release from the endoplasmic reticulum (ER) and participates in calcium oscillations (PubMed:11955285, PubMed:12442173, PubMed:20813840, PubMed:2554142, PubMed:28416699, PubMed:35568199, PubMed:38099643).
Undergoes conformational changes upon ligand binding, suggesting structural flexibility that allows the channel to switch from a closed state, capable of interacting with its ligands such as inositol 1,4,5-trisphosphate and Ca2+, to an open state, capable of transferring calcium ions across the ER membrane (By similarity).
Cytoplasmic calcium, released from the ER, triggers apoptosis by the activation of CAMK2 complex (PubMed:19752026).
Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (PubMed:29907098).
Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (PubMed:23542070).
Regulates fertilization and egg activation by tuning the frequency and amplitude of calcium oscillations (PubMed:38099643).

Catalytic activity

Activity regulation

Inositol 1,4,5-trisphosphate-gated calcium channel activity is regulated by cytosolic calcium in a biphasic manner, with low concentrations causing activation and higher concentrations inhibiting channel opening, giving rise to calcium oscillations. ATP increases the open probability of IP3R1 by synergizing with the activating effect of these two primarily ligands, inositol 1,4,5-trisphosphate and calcium (By similarity).
Inositol 1,4,5-trisphosphate-gated calcium channel activity is activated by zinc ions (PubMed:38099643).
Inositol 1,4,5-trisphosphate-gated calcium channel activity is inhibited by CALM1 in a calcium-dependent manner (By similarity).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site2651D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site2671D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site2681D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site2691D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site5081D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site5111D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site5671D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site5681D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI)
Binding site747Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site1127Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site1130Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site1977Ca2+ 2 (UniProtKB | ChEBI); high affinity
Binding site2041Ca2+ 2 (UniProtKB | ChEBI); high affinity
Binding site2220ATP (UniProtKB | ChEBI)
Binding site2223ATP (UniProtKB | ChEBI)
Binding site2610ATP (UniProtKB | ChEBI)
Binding site2610Zn2+ (UniProtKB | ChEBI)
Binding site2611ATP (UniProtKB | ChEBI)
Binding site2613Zn2+ (UniProtKB | ChEBI)
Binding site2630Zn2+ (UniProtKB | ChEBI)
Binding site2635ATP (UniProtKB | ChEBI)
Binding site2635Zn2+ (UniProtKB | ChEBI)
Binding site2637ATP (UniProtKB | ChEBI)
Binding site2653Ca2+ 2 (UniProtKB | ChEBI); high affinity

GO annotations

AspectTerm
Cellular Componentcalcineurin complex
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular ComponentGABA-ergic synapse
Cellular Componentmembrane
Cellular Componentneuronal cell body
Cellular Componentnuclear envelope
Cellular Componentnuclear inner membrane
Cellular Componentnucleolus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Cellular Componentplatelet dense granule membrane
Cellular Componentplatelet dense tubular network
Cellular Componentpostsynapse
Cellular Componentpostsynaptic density
Cellular Componentpresynapse
Cellular Componentprotein-containing complex
Cellular Componentsarcoplasmic reticulum
Cellular ComponentSchaffer collateral - CA1 synapse
Cellular Componentsecretory granule membrane
Cellular Componentsmooth endoplasmic reticulum membrane
Cellular Componentsynapse
Cellular Componentsynaptic membrane
Cellular Componenttransport vesicle membrane
Molecular FunctionATP binding
Molecular Functioncalcium channel inhibitor activity
Molecular Functioncalcium ion binding
Molecular Functionidentical protein binding
Molecular Functioninositol 1,4,5 trisphosphate binding
Molecular Functioninositol 1,4,5-trisphosphate receptor activity involved in regulation of postsynaptic cytosolic calcium levels
Molecular Functioninositol 1,4,5-trisphosphate-gated calcium channel activity
Molecular Functionintracellularly gated calcium channel activity
Molecular Functionphosphatidylinositol binding
Molecular Functionprotein domain specific binding
Molecular Functionprotein homodimerization activity
Molecular Functionprotein phosphatase binding
Molecular Functionprotein-containing complex binding
Molecular Functiontransmembrane transporter binding
Biological Processcalcium import into the mitochondrion
Biological Processcalcium ion transport
Biological Processcell morphogenesis
Biological Processcellular response to cAMP
Biological Processendoplasmic reticulum calcium ion homeostasis
Biological Processepithelial fluid transport
Biological Processintrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
Biological Procession channel modulating, G protein-coupled receptor signaling pathway
Biological Processligand-gated ion channel signaling pathway
Biological Processliver regeneration
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of calcium-mediated signaling
Biological Processphospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
Biological Processphospholipase C-activating G protein-coupled receptor signaling pathway
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of calcium ion transport
Biological Processpositive regulation of cytosolic calcium ion concentration
Biological Processpositive regulation of hepatocyte proliferation
Biological Processpositive regulation of insulin secretion
Biological Processpositive regulation of neuron projection development
Biological Processpost-embryonic development
Biological Processprotein homotetramerization
Biological Processregulation of cytosolic calcium ion concentration
Biological Processrelease of sequestered calcium ion into cytosol
Biological Processrelease of sequestered calcium ion into cytosol by endoplasmic reticulum
Biological Processresponse to hypoxia
Biological Processsingle fertilization
Biological Processvoluntary musculoskeletal movement

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
  • Alternative names
    • IP3 receptor isoform 1 (IP3R 1; InsP3R1
      )
    • Inositol 1,4,5 trisphosphate receptor
    • Inositol 1,4,5-trisphosphate receptor type 1
    • Inositol 1,4,5-trisphosphate-binding protein P400
    • Protein PCD-6

Gene names

    • Name
      Itpr1
    • Synonyms
      Insp3r
      , Pcd6
      , Pcp1

Organism names

  • Taxonomic identifier
  • Strains
    • ICR
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P11881
  • Secondary accessions
    • P20943
    • Q99LG5

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-2273Cytoplasmic
Transmembrane2274-2294Helical
Topological domain2295-2305Lumenal
Transmembrane2306-2326Helical
Topological domain2327-2352Cytoplasmic
Transmembrane2353-2373Helical
Topological domain2374-2396Lumenal
Transmembrane2397-2417Helical
Topological domain2418-2439Cytoplasmic
Transmembrane2440-2460Helical
Topological domain2461-2569Lumenal
Transmembrane2570-2590Helical
Topological domain2591-2749Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis56Strongly reduced palmitoylation; when associated with A-849 and A-2215.
Mutagenesis167Nearly abolishes calcium flux.
Mutagenesis168Reduces calcium flux by about 50%.
Mutagenesis169Reduces calcium flux by about 50%.
Mutagenesis267Abolishes inositol 1,4,5-triphosphate binding.
Mutagenesis567Abolishes inositol 1,4,5-triphosphate binding.
Mutagenesis849Strongly reduced palmitoylation; when associated with A-56 and A-2215.
Mutagenesis1588Increases interaction with AHCYL1; when associated with A-1755.
Mutagenesis1588Decreases interaction with AHCYL1; when associated with A-1755.
Mutagenesis1755Increases interaction with AHCYL1; when associated with A-1588.
Mutagenesis1755Decreases interaction with AHCYL1; when associated with A-1588.
Mutagenesis2215Strongly reduced palmitoylation; when associated with A-56 and A-849.
Mutagenesis2463-2464Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Does not affect ERLIN2 binding.
Mutagenesis2463-2464Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2464-2465Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of ERLIN2 binding.
Mutagenesis2465Loss of the vast majority of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of ERLIN2 binding.
Mutagenesis2465-2467Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of ERLIN2 binding.
Mutagenesis2465-2467Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2468-2470Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2471Does not affect binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2471-2472Loss of binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Does not affect homotetramerization.
Mutagenesis2471-2472Loss of binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of polyubiquitination.
Mutagenesis2471-2472Does not affect binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2471-2472Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2472Does not affect binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2496No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44.
Mutagenesis2504No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44.
Mutagenesis2527Complete loss of channel activity. Significant decrease of interaction with ERP44.
Mutagenesis2550Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.
Mutagenesis2596Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 116 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, lipidation, cross-link, modified residue, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001539211-2749Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
Lipidation56S-palmitoyl cysteine
Lipidation849S-palmitoyl cysteine
Cross-link916Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link962Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link1571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue1588Phosphoserine
Modified residue1755Phosphoserine; by PKA
Cross-link1771Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link1884Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link1885Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link1886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link1901Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link1924Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link2118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link2257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Disulfide bond2527↔2533

Post-translational modification

Polyubiquitinated (PubMed:35568199).
Polyubiquitination targets ITPR1 for proteasomal degradation (PubMed:35568199).
Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked (By similarity).
Phosphorylation by cAMP kinase (PKA) enhances calcium release (By similarity).
Phosphorylation by PKA increases the interaction with inositol 1,4,5-trisphosphate and decreases the interaction with AHCYL1 (Probable)
Phosphorylated on tyrosine residues.
Palmitoylated by ZDHHC6 in immune cells, leading to regulation of ITPR1 stability and function (PubMed:25368151).

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer (PubMed:28416699).
Homotetramer (PubMed:35568199).
Interacts with ERP44 in a pH-, redox state- and calcium-dependent manner which results in the inhibition the calcium channel activity (PubMed:15652484).
The strength of this interaction inversely correlates with calcium concentration (PubMed:15652484).
Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 (By similarity).
Interacts with IRAG1 (PubMed:16990611).
Interacts with CABP1 (via N-terminus) (By similarity).
Interacts with TESPA1 (PubMed:23650607).
Interacts (when not phosphorylated) with AHCYL1 (when phosphorylated); the interaction suppresses inositol 1,4,5-trisphosphate binding to ITPR1 and is increased in the presence of BCL2L10 (PubMed:12525476, PubMed:16527252, PubMed:23542070).
Interacts with AHCYL2 (with lower affinity than with AHCYL1). Interacts with BCL2L10; the interaction is increased in the presence of AHCLY1 (By similarity).
Interacts with BOK (via BH4 domain); protects ITPR1 from proteolysis by CASP3 during apoptosis (PubMed:23884412).
Interacts with TRPC4 (By similarity).
Interacts with CHGA and CHGB (By similarity).
Interacts with CALM1; this interaction inhibits inositol 1,4,5 trisphosphate binding in both the presence and absence of calcium and Inositol 1,4,5-trisphosphate-induced calcium release in the presence of calcium (PubMed:10620513, PubMed:11955285).
Interacts with the complex composed by ERLIN1, ERLIN2 and RNF170 through ERLIN2; this interaction triggers its ubiquitin-proteasomal degradation (PubMed:35568199).
Interacts with HSPA9; this interaction couples ITPR1 to VDAC1 (By similarity).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain112-166MIR 1
Domain173-223MIR 2
Domain231-287MIR 3
Domain294-373MIR 4
Domain379-435MIR 5
Region1005-1026Disordered
Compositional bias1006-1023Polar residues
Region1136-1167Disordered
Compositional bias1145-1163Basic and acidic residues
Region1695-1730Disordered
Compositional bias1705-1719Polar residues
Region1751-1788Disordered
Region1881-1906Disordered
Region1932-1952Disordered
Region2463-2528Interaction with ERP44
Region2721-2749Disordered

Domain

The ITPR1 structure has a large solenoid CY assembly built around the central helical bundle made of the C-terminal domains from four IP3R1 subunits. The solenoid scaffold includes domains responsible for binding of ligands and regulatory proteins and is connected via an allosteric nexus at the cytosolic-membrane interface to the transmembrane channel assembly. Six transmembrane helices from each subunit form the central ion-conduction pore.

Sequence similarities

Belongs to the InsP3 receptor family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (8)
  • Sequence status
    Complete

This entry describes 8 isoforms produced by Alternative splicing. There is a combination of two alternatively spliced domains at site SI and site SII (A, B and C). Experimental confirmation may be lacking for some isoforms.

P11881-1

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.

  • Name
    1
  • Synonyms
    SISIIABC
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    2,749
  • Mass (Da)
    313,167
  • Last updated
    2010-11-30 v2
  • Checksum
    FC4CF3ABB85EB82B
MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDILSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGTSKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTALNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDESENAELPQAPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSSSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA

P11881-2

  • Name
    2
  • Synonyms
    SI-SIIABC
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P11881-3

  • Name
    3
  • Synonyms
    SISIIAC
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P11881-4

P11881-5

P11881-6

P11881-7

P11881-8

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0N4SVN2A0A0N4SVN2_MOUSEItpr1225
A0A0N4SWI0A0A0N4SWI0_MOUSEItpr1215
A0A0N4SWH7A0A0N4SWH7_MOUSEItpr1313
A0A0N4SW22A0A0N4SW22_MOUSEItpr1152
A0A1D5RLA1A0A1D5RLA1_MOUSEItpr1213

Sequence caution

The sequence AAA88319.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAH03271.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_002691318-332in isoform 2, isoform 4, isoform 6 and isoform 8
Compositional bias1006-1023Polar residues
Compositional bias1145-1163Basic and acidic residues
Sequence conflict1264in Ref. 1; CAA33433
Alternative sequenceVSP_0026921692-1714in isoform 7 and isoform 8
Compositional bias1705-1719Polar residues
Alternative sequenceVSP_0026931715in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8
Alternative sequenceVSP_0026941716-1731in isoform 5, isoform 6, isoform 7 and isoform 8
Sequence conflict2675in Ref. 1; CAA33433

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X15373
EMBL· GenBank· DDBJ
CAA33433.1
EMBL· GenBank· DDBJ
mRNA
AC120411
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC153986
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC156506
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
M75986
EMBL· GenBank· DDBJ
AAA39316.1
EMBL· GenBank· DDBJ
Genomic DNA
M75987
EMBL· GenBank· DDBJ
AAA39317.1
EMBL· GenBank· DDBJ
Genomic DNA
BC003271
EMBL· GenBank· DDBJ
AAH03271.1
EMBL· GenBank· DDBJ
mRNA Different initiation
M21530
EMBL· GenBank· DDBJ
AAA88319.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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