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Entry version 166 (18 Sep 2019)
Sequence version 2 (01 Mar 1992)
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Protein

Tenascin

Gene

TNC

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tenascin
Short name:
TN
Alternative name(s):
Cytotactin
GMEM
GP 150-225
Glioma-associated-extracellular matrix antigen
Hexabrachion
JI
Myotendinous antigen
Neuronectin
Tenascin-C
Short name:
TN-C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TNC
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiGallus gallus (Chicken)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9031 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22Add BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000774323 – 33Add BLAST11
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000774434 – 1808TenascinAdd BLAST1775

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi64InterchainPROSITE-ProRule annotation
Glycosylationi168N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi186N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi192 ↔ 202By similarity
Disulfide bondi196 ↔ 207By similarity
Disulfide bondi209 ↔ 218By similarity
Disulfide bondi223 ↔ 233By similarity
Disulfide bondi227 ↔ 238By similarity
Disulfide bondi240 ↔ 249By similarity
Disulfide bondi254 ↔ 264By similarity
Disulfide bondi258 ↔ 269By similarity
Disulfide bondi271 ↔ 280By similarity
Disulfide bondi285 ↔ 295By similarity
Disulfide bondi289 ↔ 300By similarity
Disulfide bondi302 ↔ 311By similarity
Disulfide bondi316 ↔ 326By similarity
Disulfide bondi320 ↔ 331By similarity
Glycosylationi328N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi333 ↔ 342By similarity
Disulfide bondi347 ↔ 357By similarity
Disulfide bondi351 ↔ 362By similarity
Disulfide bondi364 ↔ 373By similarity
Disulfide bondi378 ↔ 388By similarity
Disulfide bondi382 ↔ 393By similarity
Disulfide bondi395 ↔ 404By similarity
Disulfide bondi409 ↔ 419By similarity
Disulfide bondi413 ↔ 424By similarity
Disulfide bondi426 ↔ 435By similarity
Disulfide bondi440 ↔ 450By similarity
Disulfide bondi444 ↔ 455By similarity
Disulfide bondi457 ↔ 466By similarity
Disulfide bondi471 ↔ 481By similarity
Disulfide bondi475 ↔ 486By similarity
Disulfide bondi488 ↔ 497By similarity
Disulfide bondi502 ↔ 512By similarity
Disulfide bondi506 ↔ 517By similarity
Disulfide bondi519 ↔ 528By similarity
Disulfide bondi533 ↔ 543By similarity
Disulfide bondi537 ↔ 548By similarity
Disulfide bondi550 ↔ 559By similarity
Disulfide bondi564 ↔ 574By similarity
Disulfide bondi568 ↔ 579By similarity
Disulfide bondi581 ↔ 590By similarity
Glycosylationi603N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi643N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi751N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi759N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1050N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1090N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1101N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1112N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1183N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1416N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1736N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1769N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P10039

PRoteomics IDEntifications database

More...
PRIDEi
P10039

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By TGF-beta.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer; disulfide-linked. A homotrimer may be formed in the triple coiled-coil region and may be stabilized by disulfide rings at both ends. Two of such half-hexabrachions may be disulfide linked within the central globule.

Interacts with CSPG4.

2 Publications

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P10039, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000011509

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11808
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P10039

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10039

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini176 – 188EGF-like 1; incompletePROSITE-ProRule annotationAdd BLAST13
Domaini188 – 219EGF-like 2PROSITE-ProRule annotationAdd BLAST32
Domaini219 – 250EGF-like 3PROSITE-ProRule annotationAdd BLAST32
Domaini250 – 281EGF-like 4PROSITE-ProRule annotationAdd BLAST32
Domaini281 – 312EGF-like 5PROSITE-ProRule annotationAdd BLAST32
Domaini312 – 343EGF-like 6PROSITE-ProRule annotationAdd BLAST32
Domaini343 – 374EGF-like 7PROSITE-ProRule annotationAdd BLAST32
Domaini374 – 405EGF-like 8PROSITE-ProRule annotationAdd BLAST32
Domaini405 – 436EGF-like 9PROSITE-ProRule annotationAdd BLAST32
Domaini436 – 467EGF-like 10PROSITE-ProRule annotationAdd BLAST32
Domaini467 – 498EGF-like 11PROSITE-ProRule annotationAdd BLAST32
Domaini498 – 529EGF-like 12PROSITE-ProRule annotationAdd BLAST32
Domaini529 – 560EGF-like 13PROSITE-ProRule annotationAdd BLAST32
Domaini560 – 591EGF-like 14PROSITE-ProRule annotationAdd BLAST32
Domaini595 – 685Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST91
Domaini686 – 775Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST90
Domaini776 – 866Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST91
Domaini867 – 957Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST91
Domaini958 – 1046Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST89
Domaini1047 – 1138Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST92
Domaini1139 – 1228Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST90
Domaini1229 – 1318Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST90
Domaini1319 – 1408Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST90
Domaini1409 – 1495Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST87
Domaini1496 – 1584Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST89
Domaini1582 – 1797Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST216

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili118 – 142Sequence analysisAdd BLAST25

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The fibrinogen C-terminal domain mediates interaction with CSPG5.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the tenascin family.Curated

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1225 Eukaryota
KOG2579 Eukaryota
ENOG4111MDJ LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10039

Database of Orthologous Groups

More...
OrthoDBi
18592at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063 FN3, 11 hits
cd00087 FReD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 11 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR013111 EGF_extracell
IPR041161 EGF_Tenascin
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07974 EGF_2, 3 hits
PF18720 EGF_Tenascin, 9 hits
PF00147 Fibrinogen_C, 1 hit
PF00041 fn3, 11 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181 EGF, 13 hits
SM00186 FBG, 1 hit
SM00060 FN3, 11 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265 SSF49265, 8 hits
SSF56496 SSF56496, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00022 EGF_1, 14 hits
PS01186 EGF_2, 14 hits
PS50026 EGF_3, 5 hits
PS51406 FIBRINOGEN_C_2, 1 hit
PS50853 FN3, 11 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Isoforms are produced in a tissue- and time-specific manner during development.
Isoform 1 (identifier: P10039-1) [UniParc]FASTAAdd to basket
Also known as: 230 kDa

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MGLPSQVLAC AILGLLYQHA SGGLIKRIIR QKRETGLNVT LPEDNQPVVF
60 70 80 90 100
NHVYNIKLPV GSLCSVDLDT ASGDADLKAE IEPVKNYEEH TVNEGNQIVF
110 120 130 140 150
THRINIPRRA CGCAAAPDIK DLLSRLEELE GLVSSLREQC ASGAGCCPNS
160 170 180 190 200
QTAEGRLDTA PYCSGHGNYS TEICGCVCEP GWKGPNCSEP ACPRNCLNRG
210 220 230 240 250
LCVRGKCICE EGFTGEDCSQ AACPSDCNDQ GKCVDGVCVC FEGYTGPDCG
260 270 280 290 300
EELCPHGCGI HGRCVGGRCV CHEGFTGEDC NEPLCPNNCH NRGRCVDNEC
310 320 330 340 350
VCDEGYTGED CGELICPNDC FDRGRCINGT CFCEEGYTGE DCGELTCPNN
360 370 380 390 400
CNGNGRCENG LCVCHEGFVG DDCSQKRCPK DCNNRGHCVD GRCVCHEGYL
410 420 430 440 450
GEDCGELRCP NDCHNRGRCI NGQCVCDEGF IGEDCGELRC PNDCHNRGRC
460 470 480 490 500
VNGQCECHEG FIGEDCGELR CPNDCNSHGR CVNGQCVCDE GYTGEDCGEL
510 520 530 540 550
RCPNDCHNRG RCVEGRCVCD NGFMGEDCGE LSCPNDCHQH GRCVDGRCVC
560 570 580 590 600
HEGFTGEDCR ERSCPNDCNN VGRCVEGRCV CEEGYMGIDC SDVSPPTELT
610 620 630 640 650
VTNVTDKTVN LEWKHENLVN EYLVTYVPTS SGGLDLQFTV PGNQTSATIH
660 670 680 690 700
ELEPGVEYFI RVFAILKNKK SIPVSARVAT YLPAPEGLKF KSVRETSVQV
710 720 730 740 750
EWDPLSISFD GWELVFRNMQ KKDDNGDITS SLKRPETSYM QPGLAPGQQY
760 770 780 790 800
NVSLHIVKNN TRGPGLSRVI TTKLDAPSQI EAKDVTDTTA LITWSKPLAE
810 820 830 840 850
IEGIELTYGP KDVPGDRTTI DLSEDENQYS IGNLRPHTEY EVTLISRRGD
860 870 880 890 900
MESDPAKEVF VTDLDAPRNL KRVSQTDNSI TLEWKNSHAN IDNYRIKFAP
910 920 930 940 950
ISGGDHTELT VPKGNQATTR ATLTGLRPGT EYGIGVTAVR QDRESAPATI
960 970 980 990 1000
NAGTDLDNPK DLEVSDPTET TLSLRWRRPV AKFDRYRLTY VSPSGKKNEM
1010 1020 1030 1040 1050
EIPVDSTSFI LRGLDAGTEY TISLVAEKGR HKSKPTTIKG STEEEPELGN
1060 1070 1080 1090 1100
LSVSETGWDG FQLTWTAADG AYENFVIQVQ QSDNPEETWN ITVPGGQHSV
1110 1120 1130 1140 1150
NVTGLKANTP YNVTLYGVIR GYRTKPLYVE TTTGAHPEVG ELTVSDITPE
1160 1170 1180 1190 1200
SFNLSWTTTN GDFDAFTIEI IDSNRLLEPM EFNISGNSRT AHISGLSPST
1210 1220 1230 1240 1250
DFIVYLYGIS HGFRTQAISA AATTEAEPEV DNLLVSDATP DGFRLSWTAD
1260 1270 1280 1290 1300
DGVFDSFVLK IRDTKRKSDP LELIVPGHER THDITGLKEG TEYEIELYGV
1310 1320 1330 1340 1350
SSGRRSQPIN SVATTVVGSP KGISFSDITE NSATVSWTPP RSRVDSYRVS
1360 1370 1380 1390 1400
YVPITGGTPN VVTVDGSKTR TKLVKLVPGV DYNVNIISVK GFEESEPISG
1410 1420 1430 1440 1450
ILKTALDSPS GLVVMNITDS EALATWQPAI AAVDNYIVSY SSEDEPEVTQ
1460 1470 1480 1490 1500
MVSGNTVEYD LNGLRPATEY TLRVHAVKDA QKSETLSTQF TTGLDAPKDL
1510 1520 1530 1540 1550
SATEVQSETA VITWRPPRAP VTDYLLTYES IDGRVKEVIL DPETTSYTLT
1560 1570 1580 1590 1600
ELSPSTQYTV KLQALSRSMR SKMIQTVFTT TGLLYPYPKD CSQALLNGEV
1610 1620 1630 1640 1650
TSGLYTIYLN GDRTQPLQVF CDMAEDGGGW IVFLRRQNGK EDFYRNWKNY
1660 1670 1680 1690 1700
VAGFGDPKDE FWIGLENLHK ISSQGQYELR VDLRDRGETA YAVYDKFSVG
1710 1720 1730 1740 1750
DAKTRYRLRV DGYSGTAGDS MTYHNGRSFS TFDKDNDSAI TNCALSYKGA
1760 1770 1780 1790 1800
FWYKNCHRVN LMGRYGDNNH SQGVNWFHWK GHEYSIQFAE MKLRPSSFRN

LEGRRKRA
Length:1,808
Mass (Da):198,859
Last modified:March 1, 1992 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB924A06CF9EFD6DE
GO
Isoform 2 (identifier: P10039-2) [UniParc]FASTAAdd to basket
Also known as: 200 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1043-1224: Missing.

Show »
Length:1,626
Mass (Da):178,977
Checksum:i3C85565BA96A21B7
GO
Isoform 3 (identifier: P10039-3) [UniParc]FASTAAdd to basket
Also known as: 190 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1043-1315: Missing.

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Length:1,535
Mass (Da):168,905
Checksum:iD7019911B76F1F4D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti182W → R in CAA30824 (PubMed:2460335).Curated1
Sequence conflicti563 – 571SCPNDCNNV → PAPMTATTW in AAA48748 (PubMed:2451243).Curated9
Sequence conflicti598E → G in AAA48748 (PubMed:2451243).Curated1
Sequence conflicti838T → TEY in AAA48748 (PubMed:2451243).Curated1
Sequence conflicti886N → F in AAA48748 (PubMed:2451243).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0014111043 – 1315Missing in isoform 3. 1 PublicationAdd BLAST273
Alternative sequenceiVSP_0014101043 – 1224Missing in isoform 2. 1 PublicationAdd BLAST182

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M23121 mRNA Translation: AAA49086.1
X08031 mRNA Translation: CAB40811.1
X08030 mRNA Translation: CAA30824.1 Different termination.
J03641 mRNA Translation: AAA48748.1 Sequence problems.
M20816 mRNA Translation: AAA48749.1 Sequence problems.

Protein sequence database of the Protein Information Resource

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PIRi
A31930

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23121 mRNA Translation: AAA49086.1
X08031 mRNA Translation: CAB40811.1
X08030 mRNA Translation: CAA30824.1 Different termination.
J03641 mRNA Translation: AAA48748.1 Sequence problems.
M20816 mRNA Translation: AAA48749.1 Sequence problems.
PIRiA31930

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QR4X-ray2.55A/B950-1042[»]
A/B1316-1408[»]
SMRiP10039
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP10039, 1 interactor
STRINGi9031.ENSGALP00000011509

Proteomic databases

PaxDbiP10039
PRIDEiP10039

Phylogenomic databases

eggNOGiKOG1225 Eukaryota
KOG2579 Eukaryota
ENOG4111MDJ LUCA
InParanoidiP10039
OrthoDBi18592at2759

Miscellaneous databases

EvolutionaryTraceiP10039

Family and domain databases

CDDicd00063 FN3, 11 hits
cd00087 FReD, 1 hit
Gene3Di2.60.40.10, 11 hits
InterProiView protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR013111 EGF_extracell
IPR041161 EGF_Tenascin
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
PfamiView protein in Pfam
PF07974 EGF_2, 3 hits
PF18720 EGF_Tenascin, 9 hits
PF00147 Fibrinogen_C, 1 hit
PF00041 fn3, 11 hits
SMARTiView protein in SMART
SM00181 EGF, 13 hits
SM00186 FBG, 1 hit
SM00060 FN3, 11 hits
SUPFAMiSSF49265 SSF49265, 8 hits
SSF56496 SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS00022 EGF_1, 14 hits
PS01186 EGF_2, 14 hits
PS50026 EGF_3, 5 hits
PS51406 FIBRINOGEN_C_2, 1 hit
PS50853 FN3, 11 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTENA_CHICK
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P10039
Secondary accession number(s): O73584, O73585, P13132
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 1, 1992
Last modified: September 18, 2019
This is version 166 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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