Q5H8C1 · FREM1_HUMAN
- ProteinFRAS1-related extracellular matrix protein 1
- GeneFREM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2179 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development.
Miscellaneous
Was termed QBRICK because it contains 12 repeats: 'Q' stands for queen and is taken from the queen being the 12th in a suit of playing card, and 'BRICK' stands for the repeating unit.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | basement membrane | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | metal ion binding | |
Biological Process | anatomical structure morphogenesis | |
Biological Process | cell communication | |
Biological Process | cell-matrix adhesion | |
Biological Process | craniofacial suture morphogenesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFRAS1-related extracellular matrix protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5H8C1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes at the basement membrane zone of embryonic epidermis and hair follicles.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Bifid nose, with or without anorectal and renal anomalies (BNAR)
- Note
- DescriptionA disease characterized by the presence of a bifid nose usually associated with renal agenesis and anorectal malformations. A bifid nose is a congenital deformity due to failure of the paired nasal processes to fuse to a single midline organ during early gestation.
- See alsoMIM:608980
Natural variants in BNAR
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_063422 | 649 | R>W | in BNAR; dbSNP:rs121912609 | |
VAR_063423 | 1440 | G>S | in BNAR; dbSNP:rs121912610 |
Manitoba oculotrichoanal syndrome (MOTA)
- Note
- DescriptionA rare condition defined by eyelid colobomas, cryptophthalmos, and anophthalmia/microphthalmia, an aberrant hairline, a bifid or broad nasal tip, and gastrointestinal anomalies such as omphalocele and anal stenosis.
- See alsoMIM:248450
Natural variants in MOTA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078339 | 102 | D>G | in MOTA; uncertain significance; dbSNP:rs1338652795 | |
VAR_066412 | 1324 | L>R | in MOTA; dbSNP:rs281875281 | |
VAR_066413 | 2091 | V>I | in MOTA; dbSNP:rs281875282 |
Trigonocephaly 2 (TRIGNO2)
- Note
- DescriptionA keel-shaped deformation of the forehead, caused by premature fusion of the metopic sutures. It results in a triangular shape of the head.
- See alsoMIM:614485
Natural variants in TRIGNO2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067916 | 498 | R>Q | in TRIGNO2; dbSNP:rs184394424 | |
VAR_067917 | 1500 | E>V | in TRIGNO2; dbSNP:rs281875280 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_078339 | 102 | in MOTA; uncertain significance; dbSNP:rs1338652795 | |||
Sequence: D → G | ||||||
Natural variant | VAR_047317 | 439 | in dbSNP:rs2779500 | |||
Sequence: V → L | ||||||
Natural variant | VAR_067916 | 498 | in TRIGNO2; dbSNP:rs184394424 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_047318 | 499 | in dbSNP:rs1353223 | |||
Sequence: I → V | ||||||
Natural variant | VAR_063422 | 649 | in BNAR; dbSNP:rs121912609 | |||
Sequence: R → W | ||||||
Natural variant | VAR_047319 | 803 | in dbSNP:rs7023244 | |||
Sequence: S → Y | ||||||
Natural variant | VAR_047320 | 863 | in dbSNP:rs7041710 | |||
Sequence: L → V | ||||||
Natural variant | VAR_047321 | 1202 | in dbSNP:rs16932300 | |||
Sequence: S → R | ||||||
Natural variant | VAR_047322 | 1273 | in dbSNP:rs7025814 | |||
Sequence: D → E | ||||||
Natural variant | VAR_066412 | 1324 | in MOTA; dbSNP:rs281875281 | |||
Sequence: L → R | ||||||
Natural variant | VAR_063423 | 1440 | in BNAR; dbSNP:rs121912610 | |||
Sequence: G → S | ||||||
Natural variant | VAR_067917 | 1500 | in TRIGNO2; dbSNP:rs281875280 | |||
Sequence: E → V | ||||||
Natural variant | VAR_047323 | 1502 | in dbSNP:rs10961700 | |||
Sequence: V → M | ||||||
Natural variant | VAR_047324 | 1576 | in dbSNP:rs2101770 | |||
Sequence: N → I | ||||||
Natural variant | VAR_066413 | 2091 | in MOTA; dbSNP:rs281875282 | |||
Sequence: V → I | ||||||
Natural variant | VAR_047325 | 2143 | in dbSNP:rs10961689 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_047326 | 2174 | in dbSNP:rs17856912 | |||
Sequence: V → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,667 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MNSLSWGAANAVLLLLLLAWA | ||||||
Chain | PRO_0000010122 | 22-2179 | FRAS1-related extracellular matrix protein 1 | |||
Sequence: SPTFISINRGVRVMKGHSAFLSGDDLKFAIPKEKDACKVEVVMNEPITQRVGKLTPQVFDCHFLPNEVKYVHNGCPILDEDTVKLRLYRFTERDTFIETFILWVYLLEPDCNIIHMSNNVLEVPEFNGLSQAIDKNLLRFDYDRMASLECTVSLDTARTRLPAHGQMVLGEPRPEEPRGDQPHSFFPESQLRAKLKCPGGSCTPGLKKIGSLKVSCEEFLLMGLRYQHLDPPSPNIDYISIQLDLTDTRSKIVYKSESAWLPVYIRAGIPNQIPKAAFMAVFILEVDQFILTSLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQIAYQPPNSSHSERRHDEVELEVYDFFFERSAPMTVHISIRTADTNAPRVSWNTGLSLLEGQSRAITWEQFQVVDNDDIGAVRLVTVGGLQHGWLTLRGGKGFLFTVADLQAGVVRYHHDDSDSTKDFVVFRIFDGHHSIRHKFPINVLPKDDSPPFLITNVVIELEEGQTILIQGSMLRASDVDASDDYIFFNITKPPQAGEIMKKPGPGLIGYPVHGFLQRDLFNGIIYYRHFGGEIFEDSFQFVLWDSHEPPNLSVPQVATIHITPVDDQLPKEAPGVSRHLVVKETEVAYITKKQLHFIDSESYDRELVYTITTPPFFSFSHRHLDAGKLFMVDSIPKVVKNPTALELRSFTQHAVNYMKVAYMPPMQDIGPHCRDVQFTFSVSNQHGGTLHGICFNITILPVDNQVPEAFTNPLKVTEGGQSIISTEHILISDADTKLDNIDLSLRELPLHGRVELNGFPLNSGGTFSWGDLHTLKVRYQHDGTEVLQDDLLLEVTDGTNSAEFVLHVEVFPVNDEPPVLKADLMPVMNCSEGGEVVITSEYIFATDVDSDNLKLMFVIAREPQHGVVRRAGVTVDQFSQRDVISEAVTYKHTGGEIGLMPCFDTITLVVSDGEAGPFVNGCCYNGPNPSVPLHASFPVYDLNITVYPVDNQPPSIAIGPVFVVDEGCSTALTVNHLSATDPDTAADDLEFVLVSPPQFGYLENILPSVGFEKSNIGISIDSFQWKDMNAFHINYVQSRHLRIEPTADQFTVYVTDGKHHSLEIPFSIIINPTNDEAPDFVVQNITVCEGQMKELDSSIISAVDLDIPQDALLFSITQKPRHGLLIDRGFSKDFSENKQPANPHQKHAPVHSFSMELLKTGMRLTYMHDDSESLADDFTIQLSDGKHKILKTISVEVIPVNDEKPMLSKKAEIAMNMGETRIISSAILSAIDEDSPREKIYYVFERLPQNGQLQLKIGRDWVPLSPGMKCTQEEVDLNLLRYTHTGAMDSQNQDSFTFYLWDGNNRSPALDCQITIKDMEKGDIVILTKPLVVSKGDRGFLTTTTLLAVDGTDKPEELLYVITSPPRYGQIEYVHYPGVPITNFSQMDVVGQTVCYVHKSKVTVSSDRFRFIISNGLRTEHGVFEITLETVDRALPVVTRNKGLRLAQGAVGLLSPDLLQLTDPDTPAENLTFLLVQLPQHGQLYLWGTGLLQHNFTQQDVDSKNVAYRHSGGDSQTDCFTFMATDGTNQGFIVNGRVWEEPVLFTIQVDQLDKTAPRITLLHSPSQVGLLKNGCYGIYITSRVLKASDPDTEDDQIIFKILQGPKHGHLENTTTGEFIHEKFSQKDLNSKTILYIINPSLEVNSDTVEFQIMDPTGNSATPQILELKWSHIEWSQTEYEVCENVGLLPLEIIRRGYSMDSAFVGIKVNQVSAAVGKDFTVIPSKLIQFDPGMSTKMWNIAITYDGLEEDDEVFEVILNSPVNAVLGTKTKAAVKILDSKGGQCHPSYSSNQSKHSTWEKGIWHLLPPGSSSSTTSGSFHLERRPLPSSMQLAVIRGDTLRGFDSTDLSQRKLRTRGNGKTVRPSSVYRNGTDIIYNYHGIVSLKLEDDSFPTHKRKAKVSIISQPQKTIKVAELPQADKVESTTDSHFPRQDQLPSFPKNCTLELKGLFHFEEGIQKLYQCNGIAWKAWSPQTKDVEDKSCPAGWHQHSGYCHILITEQKGTWNAAAQACREQYLGNLVTVFSRQHMRWLWDIGGRKSFWIGLNDQVHAGHWEWIGGEPVAFTNGRRGPSQRSKLGKSCVLVQRQGKWQTKDCRRAKPHNYVCSRKL | ||||||
Glycosylation | 335 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 560 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 622 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1014 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1566 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2151↔2165 | |||||
Sequence: CVLVQRQGKWQTKDC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with FREM2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5H8C1 | FREM2 Q5SZK8 | 2 | EBI-21460642, EBI-20737564 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 199-201 | Cell attachment site | ||||
Sequence: RGD | ||||||
Repeat | 296-390 | CSPG 1 | ||||
Sequence: KAAFMAVFILEVDQFILTSLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQIAYQPPNSSHSERRHDEVELEVY | ||||||
Repeat | 413-500 | CSPG 2 | ||||
Sequence: APRVSWNTGLSLLEGQSRAITWEQFQVVDNDDIGAVRLVTVGGLQHGWLTLRGGKGFLFTVADLQAGVVRYHHDDSDSTKDFVVFRIF | ||||||
Repeat | 521-615 | CSPG 3 | ||||
Sequence: PPFLITNVVIELEEGQTILIQGSMLRASDVDASDDYIFFNITKPPQAGEIMKKPGPGLIGYPVHGFLQRDLFNGIIYYRHFGGEIFEDSFQFVLW | ||||||
Repeat | 642-754 | CSPG 4 | ||||
Sequence: KEAPGVSRHLVVKETEVAYITKKQLHFIDSESYDRELVYTITTPPFFSFSHRHLDAGKLFMVDSIPKVVKNPTALELRSFTQHAVNYMKVAYMPPMQDIGPHCRDVQFTFSVS | ||||||
Repeat | 776-867 | CSPG 5 | ||||
Sequence: QVPEAFTNPLKVTEGGQSIISTEHILISDADTKLDNIDLSLRELPLHGRVELNGFPLNSGGTFSWGDLHTLKVRYQHDGTEVLQDDLLLEVT | ||||||
Repeat | 887-982 | CSPG 6 | ||||
Sequence: EPPVLKADLMPVMNCSEGGEVVITSEYIFATDVDSDNLKLMFVIAREPQHGVVRRAGVTVDQFSQRDVISEAVTYKHTGGEIGLMPCFDTITLVVS | ||||||
Repeat | 1024-1126 | CSPG 7 | ||||
Sequence: PPSIAIGPVFVVDEGCSTALTVNHLSATDPDTAADDLEFVLVSPPQFGYLENILPSVGFEKSNIGISIDSFQWKDMNAFHINYVQSRHLRIEPTADQFTVYVT | ||||||
Repeat | 1147-1254 | CSPG 8 | ||||
Sequence: EAPDFVVQNITVCEGQMKELDSSIISAVDLDIPQDALLFSITQKPRHGLLIDRGFSKDFSENKQPANPHQKHAPVHSFSMELLKTGMRLTYMHDDSESLADDFTIQLS | ||||||
Repeat | 1275-1372 | CSPG 9 | ||||
Sequence: KPMLSKKAEIAMNMGETRIISSAILSAIDEDSPREKIYYVFERLPQNGQLQLKIGRDWVPLSPGMKCTQEEVDLNLLRYTHTGAMDSQNQDSFTFYLW | ||||||
Repeat | 1393-1485 | CSPG 10 | ||||
Sequence: GDIVILTKPLVVSKGDRGFLTTTTLLAVDGTDKPEELLYVITSPPRYGQIEYVHYPGVPITNFSQMDVVGQTVCYVHKSKVTVSSDRFRFIIS | ||||||
Repeat | 1506-1596 | CSPG 11 | ||||
Sequence: LPVVTRNKGLRLAQGAVGLLSPDLLQLTDPDTPAENLTFLLVQLPQHGQLYLWGTGLLQHNFTQQDVDSKNVAYRHSGGDSQTDCFTFMAT | ||||||
Repeat | 1628-1724 | CSPG 12 | ||||
Sequence: PRITLLHSPSQVGLLKNGCYGIYITSRVLKASDPDTEDDQIIFKILQGPKHGHLENTTTGEFIHEKFSQKDLNSKTILYIINPSLEVNSDTVEFQIM | ||||||
Domain | 1731-1830 | Calx-beta | ||||
Sequence: ATPQILELKWSHIEWSQTEYEVCENVGLLPLEIIRRGYSMDSAFVGIKVNQVSAAVGKDFTVIPSKLIQFDPGMSTKMWNIAITYDGLEEDDEVFEVILN | ||||||
Motif | 1907-1909 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 2060-2174 | C-type lectin | ||||
Sequence: HSGYCHILITEQKGTWNAAAQACREQYLGNLVTVFSRQHMRWLWDIGGRKSFWIGLNDQVHAGHWEWIGGEPVAFTNGRRGPSQRSKLGKSCVLVQRQGKWQTKDCRRAKPHNYV |
Domain
The Calx-beta domain binds calcium with high affinity and undergo a major conformational shift upon binding.
Sequence similarities
Belongs to the FRAS1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing.
Q5H8C1-1
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.
- Name1
- Length2,179
- Mass (Da)244,154
- Last updated2008-11-25 v3
- Checksum9C1C464DF95D2194
Q5H8C1-2
- Name2
- Differences from canonical
- 1-1464: Missing
- 1465-1480: VCYVHKSKVTVSSDRF → MVTQESMLKAALPLFT
Q5H8C1-3
- Name3
- Differences from canonical
- 1-1803: Missing
Q5H8C1-4
- Name4
- Differences from canonical
- 1-1587: Missing
- 1588-1619: TDCFTFMATDGTNQGFIVNGRVWEEPVLFTIQ → MLDESLAVRRSKKCKEMIMHWEKKEDIDIVNT
- 1804-1809: MSTKMW → SSILCL
- 1810-2179: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WE85 | F8WE85_HUMAN | FREM1 | 1335 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047283 | 1-1464 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015026 | 1-1587 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015025 | 1-1803 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047284 | 1465-1480 | in isoform 2 | |||
Sequence: VCYVHKSKVTVSSDRF → MVTQESMLKAALPLFT | ||||||
Alternative sequence | VSP_015029 | 1588-1619 | in isoform 4 | |||
Sequence: TDCFTFMATDGTNQGFIVNGRVWEEPVLFTIQ → MLDESLAVRRSKKCKEMIMHWEKKEDIDIVNT | ||||||
Sequence conflict | 1735 | in Ref. 5; AAH31064 | ||||
Sequence: I → N | ||||||
Alternative sequence | VSP_015030 | 1804-1809 | in isoform 4 | |||
Sequence: MSTKMW → SSILCL | ||||||
Alternative sequence | VSP_015031 | 1810-2179 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 1861 | in Ref. 3; CAE46048 | ||||
Sequence: S → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB160987 EMBL· GenBank· DDBJ | BAD89015.1 EMBL· GenBank· DDBJ | mRNA | ||
AK058190 EMBL· GenBank· DDBJ | BAB71709.1 EMBL· GenBank· DDBJ | mRNA | ||
BX641104 EMBL· GenBank· DDBJ | CAE46048.1 EMBL· GenBank· DDBJ | mRNA | ||
AL354672 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL390732 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL512643 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC031064 EMBL· GenBank· DDBJ | AAH31064.2 EMBL· GenBank· DDBJ | mRNA | Different initiation |