Tpm1 tropomyosin 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Tpm1provided by RGD
Official Full Name: tropomyosin 1provided by RGD
Primary source: RGD:3898
See related: EnsemblRapid:ENSRNOG00000018184 AllianceGenome:RGD:3898
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: Tma2; Tmsa; Alpha-tm
Summary: This gene is a member of the tropomyosin family and encodes a protein that heterodimerizes with a beta subunit, binding actin in both muscle and nonmuscle cells. In both smooth and striated muscle cells, it plays a role in calcium dependent-regulation of muscle contraction. In nonmuscle cells, it stabilizes cytoskeleton actin filaments. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008]
Expression: Biased expression in Muscle (RPKM 22251.9) and Heart (RPKM 10996.5) See more
Orthologs: human mouse all
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Genomic context

Location:: 8q24

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	8	NC_086026.1 (76516654..76543661, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	8	NC_051343.1 (67635479..67662330, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	8	NC_005107.4 (72814737..72841496, complement)

Chromosome 8 - NC_086026.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

CaMKII regulates the proteins TPM1 and MYOM2 and promotes diacetylmorphine-induced abnormal cardiac rhythms.
Title: CaMKII regulates the proteins TPM1 and MYOM2 and promotes diacetylmorphine-induced abnormal cardiac rhythms.
the R21H mutation causes a twofold decrease in tropomyosin's affinity for F-actin and affects leiomodin's function.
Title: Effects of cardiomyopathy-linked mutations K15N and R21H in tropomyosin on thin-filament regulation and pointed-end dynamics.
Hypoxia and hyperoxia differentially control proliferation of rat neural crest stem cells via distinct regulatory pathways of the HIF1alpha-CXCR4 and TP53-TPM1 proteins
Title: Hypoxia and hyperoxia differentially control proliferation of rat neural crest stem cells via distinct regulatory pathways of the HIF1α-CXCR4 and TP53-TPM1 proteins.
Transmission of stability information through the N-domain of tropomyosin is interrupted by a stabilizing mutation (A109L) in the hydrophobic core of the stability control region (residues 97-118).
Title: Transmission of stability information through the N-domain of tropomyosin is interrupted by a stabilizing mutation (A109L) in the hydrophobic core of the stability control region (residues 97-118).
the link between flexibility of TM and its function in ejecting hearts.
Title: Conserved Asp-137 is important for both structure and regulatory functions of cardiac α-tropomyosin (α-TM) in a novel transgenic mouse model expressing α-TM-D137L.
analysis of the pattern of of evolutionarily conserved basic and acidic residues that constitutes the binding interface of actin-tropomyosin
Title: A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin.
The evolutionarily conserved residues are important for actomyosin regulation, a universal function of Tm that has a common structural basis and mechanism.
Title: Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin.
troponin C (cTnC) and tropomyosin (cTm) are not only present in myofilaments of ventricular cardiomyocytes in culture but are also within their nuclei
Title: Nuclear cardiac troponin and tropomyosin are expressed early in cardiac differentiation of rat mesenchymal stem cells.
TPM1 may play an important role in the occurrence and development of liver fibrosis.
Title: [Dynamic expression of tropomyosin 1 in rat model of hepatic fibrosis and hepatic stellate cells].
The results were consistent with a mechanism in which the alpha-tropomyosin-actin interaction cooperatively affects actin to result in the generation of greater force and velocity.
Title: The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.

Submit: New GeneRIF Correction See all GeneRIFs (19)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH134075 (e-PCR)
- UniSTS:217357

RH140166 (e-PCR)
- UniSTS:222245

RH140171 (e-PCR)
- UniSTS:222250

RH136834 (e-PCR)
- UniSTS:218923

D8Mgh5 (e-PCR)
- UniSTS:119610

BE117331 (e-PCR)
- UniSTS:248667

RH138229 (e-PCR)
- UniSTS:220316

RH132196 (e-PCR)
- UniSTS:215479

RH144195 (e-PCR)
- UniSTS:233441

BE118313 (e-PCR)
- UniSTS:248809

CSAP35E (e-PCR), detects polymorphism
- UniSTS:279549

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables actin binding	IDA Inferred from Direct Assay more info	PubMed
enables actin binding	IEA Inferred from Electronic Annotation more info
enables actin binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables actin binding	TAS Traceable Author Statement more info	PubMed
enables actin filament binding	IBA Inferred from Biological aspect of Ancestor more info
enables actin filament binding	IDA Inferred from Direct Assay more info	PubMed
enables actin filament binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables actin filament binding	ISO Inferred from Sequence Orthology more info
enables cytoskeletal protein binding	ISO Inferred from Sequence Orthology more info
enables disordered domain specific binding	IPI Inferred from Physical Interaction more info	PubMed
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein heterodimerization activity	IDA Inferred from Direct Assay more info	PubMed
enables protein homodimerization activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in actin filament capping	IDA Inferred from Direct Assay more info	PubMed
involved_in actin filament organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in cardiac muscle contraction	IBA Inferred from Biological aspect of Ancestor more info
involved_in cardiac muscle contraction	IDA Inferred from Direct Assay more info	PubMed
involved_in cardiac muscle contraction	IEA Inferred from Electronic Annotation more info
involved_in cardiac muscle contraction	ISO Inferred from Sequence Orthology more info
involved_in cellular response to reactive oxygen species	IEA Inferred from Electronic Annotation more info
involved_in cellular response to reactive oxygen species	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within in utero embryonic development	ISO Inferred from Sequence Orthology more info
involved_in muscle contraction	TAS Traceable Author Statement more info	PubMed
involved_in muscle filament sliding	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of cell migration	IGI Inferred from Genetic Interaction more info	PubMed
involved_in negative regulation of vascular associated smooth muscle cell migration	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of vascular associated smooth muscle cell migration	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of vascular associated smooth muscle cell proliferation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of vascular associated smooth muscle cell proliferation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of ATP-dependent activity	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of ATP-dependent activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of cell adhesion	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of heart rate by epinephrine	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of stress fiber assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of ATP-dependent activity	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of cell shape	IEA Inferred from Electronic Annotation more info
involved_in regulation of cell shape	ISO Inferred from Sequence Orthology more info
involved_in ruffle organization	IGI Inferred from Genetic Interaction more info	PubMed
involved_in sarcomere organization	IEA Inferred from Electronic Annotation more info
involved_in sarcomere organization	ISO Inferred from Sequence Orthology more info
involved_in ventricular cardiac muscle tissue morphogenesis	IEA Inferred from Electronic Annotation more info
involved_in ventricular cardiac muscle tissue morphogenesis	ISO Inferred from Sequence Orthology more info
involved_in wound healing	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in actin cytoskeleton	IDA Inferred from Direct Assay more info	PubMed
located_in actin cytoskeleton	ISO Inferred from Sequence Orthology more info
is_active_in actin filament	IBA Inferred from Biological aspect of Ancestor more info
located_in bleb	IEA Inferred from Electronic Annotation more info
located_in bleb	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoskeleton	IEA Inferred from Electronic Annotation more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in myofibril	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed
located_in ruffle membrane	IEA Inferred from Electronic Annotation more info
located_in ruffle membrane	ISO Inferred from Sequence Orthology more info
located_in stress fiber	IEA Inferred from Electronic Annotation more info
located_in stress fiber	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: tropomyosin alpha-1 chain

Names: hepatoma alpha tropomyosin; smooth muscle alpha-tropomyosin; striated muscle alpha-tropomyosin; tropomyosin 1, alpha; tropomyosin 3 alpha; tropomyosin-alpha

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001034068.1 → NP_001029240.1 tropomyosin alpha-1 chain isoform a

See identical proteins and their annotated locations for NP_001029240.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the longest isoform (a).

Source sequence(s)

AA899493, AF372217, CB787774, M60667

UniProtKB/TrEMBL

A0A096MIT6, Q91XN6

Conserved Domains (1) summary

pfam00261
Location:48 → 259

Tropomyosin
NM_001034069.1 → NP_001029241.1 tropomyosin alpha-1 chain isoform Tpm1.6cy

See identical proteins and their annotated locations for NP_001029241.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.6, also known as variant 2) contains a different 3' exon compared to variant 1. The resulting protein (isoform Tpm1.6cy, also referred to as TM-2) is shorter and has a distinct C-terminus compared to isoform a. Isoform Tpm1.6cy is the same length as isoforms Tpm1.7cy and Tpm1.3sm but is the product of alternate splicing and contains short regions of sequence differences.

Source sequence(s)

BC078780, BU670983, M60666

UniProtKB/TrEMBL

A0A8L2UK34, A6KEY3

Related

ENSRNOP00000070151.3, ENSRNOT00000085894.3

Conserved Domains (1) summary

pfam00261
Location:48 → 282

Tropomyosin
NM_001034070.1 → NP_001029242.1 tropomyosin alpha-1 chain isoform Tpm1.7cy

See identical proteins and their annotated locations for NP_001029242.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.7, also known as variant 3) has multiple differences in the coding region, compared to variant 1, resulting in a shorter protein (isoform Tpm1.7cy, also referred to as TM-3). Isoform Tpm1.7cy is the same length as isoforms Tpm1.6cy and Tpm1.3sm but is the product of alternate splicing and contains short regions of sequence differences.

Source sequence(s)

BC078780, CB787774, CK483405, M60667

UniProtKB/TrEMBL

Q63583, Q63607

Conserved Domains (1) summary

pfam00261
Location:48 → 282

Tropomyosin
NM_001034071.1 → NP_001029243.1 tropomyosin alpha-1 chain isoform Tpm1.3sm

See identical proteins and their annotated locations for NP_001029243.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.3, also known as variant 4) has multiple differences in the coding region, compared to variant 1, resulting in a shorter protein (isoform Tpm1.3sm). Isoform Tpm1.3sm is the same length as isoforms Tpm1.6cy and Tpm1.7cy but is the product of alternate splicing and contains short regions of sequence differences.

Source sequence(s)

AF372216, BC078780, BU670983, M60667

UniProtKB/TrEMBL

F7FK40, Q923Z2

Conserved Domains (2) summary

PHA03248
Location:51 → 147

PHA03248; DNA packaging tegument protein UL25; Provisional

pfam00261
Location:48 → 282

Tropomyosin; Tropomyosin
NM_001034072.1 → NP_001029244.1 tropomyosin alpha-1 chain isoform Tpm1.10br

See identical proteins and their annotated locations for NP_001029244.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.10, also known as variant 5) contains a different 3' exon compared to variant 1. The resulting protein (isoform Tpm1.10br, also referred to as TMBr-1) is shorter and has a distinct C-terminus compared to isoform a.

Source sequence(s)

AF372217, BE118215, CB787774, M34135

UniProtKB/TrEMBL

A6KEY5

Related

ENSRNOP00000024575.7, ENSRNOT00000024575.10

Conserved Domains (1) summary

pfam00261
Location:48 → 280

Tropomyosin
NM_001034073.1 → NP_001029245.1 tropomyosin alpha-1 chain isoform Tpm1.8cy

See identical proteins and their annotated locations for NP_001029245.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.8, also known as variant 7) has multiple differences in the coding region compared to variant 1. These differences result in an isoform (Tpm1.8cy, also referred to as TM-5a) that is shorter and has distinct N- and C-termini compared to isoform a. Isoform Tpm1.8cy is the same length as isoforms Tpm1.9cy and Tpm1.13 but is the product of alternate splicing and contains short regions of sequence differences.

Source sequence(s)

BC078780, CB585296, M60668

UniProtKB/TrEMBL

A6KEZ2

Conserved Domains (1) summary

pfam00261
Location:12 → 246

Tropomyosin
NM_001034074.1 → NP_001029246.1 tropomyosin alpha-1 chain isoform Tpm1.9cy

See identical proteins and their annotated locations for NP_001029246.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.9, also known as variant 8) has multiple differences in the coding region, compared to variant 1. These differences result in an isoform (Tpm1.9cy, also referred to as TM-5b) that is shorter and has distinct N- and C-termini compared to isoform a. Isoform Tpm1.9cy is the same length as isoforms Tpm1.8cy and Tpm1.13 but is the product of alternate splicing and contains short regions of sequence differences.

Source sequence(s)

BC078780, CO562261, M34136

UniProtKB/TrEMBL

A0A0G2JSQ4, A0A9K3Y6T5, Q6AZ25

Conserved Domains (1) summary

pfam00261
Location:12 → 246

Tropomyosin
NM_001034075.1 → NP_001029247.1 tropomyosin alpha-1 chain isoform Tpm1.13

See identical proteins and their annotated locations for NP_001029247.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.13, also known as variant 9) has multiple differences in the coding region, compared to variant 1. These differences result in an isoform (Tpm1.13) that is shorter and has distinct N- and C- termini compared to isoform a. Isoform Tpm1.13 is the same length as isoforms Tpm1.8cy and Tpm1.9cy but is the product of alternate splicing and contains short regions of sequence differences.

Source sequence(s)

AA899493, AF372215, CO562261, X02412

UniProtKB/TrEMBL

A6KEZ6, Q91XN7

Conserved Domains (1) summary

pfam00261
Location:12 → 246

Tropomyosin
NM_001301336.1 → NP_001288265.1 tropomyosin alpha-1 chain isoform Tpm1.1st

See identical proteins and their annotated locations for NP_001288265.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.1st, also known as variant 10) contains a alternate 3' exon compared to variant 1. The resulting protein (isoform Tpm1.1st) is shorter and has a distinct C-terminus compared to isoform a.

Source sequence(s)

JAXUCZ010000008

UniProtKB/Swiss-Prot

P04692, P06469, P18342, P18343, P18344, P19354, Q53X09, Q63582, Q63608, Q63609

UniProtKB/TrEMBL

A0A0G2K7F7, A6KEY9

Related

ENSRNOP00000048499.3, ENSRNOT00000048044.7

Conserved Domains (1) summary

pfam00261
Location:48 → 282

Tropomyosin
NM_001301342.1 → NP_001288271.1 tropomyosin alpha-1 chain isoform Tpm1.2st

See identical proteins and their annotated locations for NP_001288271.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.2, also known as variant 11) has multiple differences in the coding region, compared to variant 1, resulting in a shorter protein (isoform Tpm1.2st). The resulting protein (isoform Tpm1.2st) is shorter and has a distinct C-terminus compared to isoform a.

Source sequence(s)

AI603512, CF108680, FQ074026, FQ217616

UniProtKB/TrEMBL

A0A8I6A156, A6KEY7

Conserved Domains (3) summary

PHA03248
Location:51 → 147

PHA03248; DNA packaging tegument protein UL25; Provisional

pfam00261
Location:48 → 282

Tropomyosin; Tropomyosin

pfam07851
Location:180 → 274

TMPIT; TMPIT-like protein
NM_001301736.1 → NP_001288665.1 tropomyosin alpha-1 chain isoform Tpm1.12br

See identical proteins and their annotated locations for NP_001288665.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.12, also known as variant 12) differs in the 5' and 3' UTRs and has multiple differences in the coding region, compared to variant 1, resulting in a shorter protein (isoform Tpm1.12br). The resulting protein (isoform Tpm1.12br) is shorter than isoform a.

Source sequence(s)

JAXUCZ010000008

UniProtKB/TrEMBL

A6KEZ3

Conserved Domains (1) summary

pfam00261
Location:12 → 244

Tropomyosin
NM_019131.2 → NP_062004.1 tropomyosin alpha-1 chain isoform Tpm1.11br

See identical proteins and their annotated locations for NP_062004.1

Status: REVIEWED

Description

Transcript Variant: This variant (Tpm1.11, also known as variant 6) has a different 5' UTR and 5' coding region compared to variant 1. The resulting protein (isoform Tpm1.11br, also referred to as TMBr-2) has a distinct N-terminus and is shorter than isoform a.

Source sequence(s)

AA899493, BC078780, CO562261, M34134

UniProtKB/TrEMBL

A6KEZ5

Conserved Domains (1) summary

pfam00261
Location:12 → 223

Tropomyosin