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Protein

Netrin receptor DCC

Gene

Dcc

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

Functioni

Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene (By similarity).By similarity1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • netrin receptor activity Source: RGD
  • transcription coactivator activity Source: RGD

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • axon guidance Source: RGD
  • netrin-activated signaling pathway Source: GOC
  • positive regulation of ERK1 and ERK2 cascade Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • regulation of nucleic acid-templated transcription Source: GOC
  • response to amphetamine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Netrin receptor DCC
Alternative name(s):
Tumor suppressor protein DCC
Gene namesi
Name:Dcc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2492. Dcc.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1100 – 112021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: RGD
  • growth cone membrane Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: RGD
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1178 – 11781S → A: Abolishes phosphorylation by MAPK1; when associated with A-1187 and A-1267. 1 Publication
Mutagenesisi1187 – 11871T → A: Abolishes phosphorylation by MAPK1; when associated with A-1178 and A-1267. 1 Publication
Mutagenesisi1267 – 12671S → A: Abolishes phosphorylation by MAPK1; when associated with A-1178 and A-1187. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 14451420Netrin receptor DCCPRO_0000416246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...)1 Publication
Disulfide bondi61 ↔ 117PROSITE-ProRule annotation1 Publication
Glycosylationi94 – 941N-linked (GlcNAc...)1 Publication
Disulfide bondi161 ↔ 212PROSITE-ProRule annotation1 Publication
Disulfide bondi261 ↔ 310PROSITE-ProRule annotation1 Publication
Glycosylationi299 – 2991N-linked (GlcNAc...)1 Publication
Glycosylationi318 – 3181N-linked (GlcNAc...)1 Publication
Disulfide bondi352 ↔ 400PROSITE-ProRule annotation1 Publication
Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence analysis
Glycosylationi628 – 6281N-linked (GlcNAc...)Sequence analysis
Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence analysis
Modified residuei1178 – 11781Phosphoserine; by MAPK11 Publication
Modified residuei1187 – 11871Phosphothreonine; by MAPK11 Publication
Modified residuei1267 – 12671Phosphoserine; by MAPK11 Publication

Post-translational modificationi

Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ63155.
PRIDEiQ63155.

PTM databases

iPTMnetiQ63155.
PhosphoSiteiQ63155.
UniCarbKBiQ63155.

Expressioni

Tissue specificityi

Detected in embryonic spinal cord, predominantly in axons of commissural neurons (at protein level). Detected in embryonic spinal cord.1 Publication

Interactioni

Subunit structurei

Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D (By similarity). Interacts with DSCAM. Interacts with PTK2/FAK1. Interacts with MYO10 (By similarity). Interacts with MAPK1. Interacts with NTN1. Interacts with CBLN4; this interaction can be competed by NTN1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1798965,EBI-1798965
Agap2Q8CGU42EBI-1798965,EBI-4409108
DscamQ9ERC84EBI-1798965,EBI-1798601From a different organism.
Robo1O550052EBI-1798965,EBI-3505237
RPL5P467774EBI-1798965,EBI-358018From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-46811N.
IntActiQ63155. 9 interactions.
STRINGi10116.ENSRNOP00000063072.

Structurei

Secondary structure

1
1445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446Combined sources
Beta strandi49 – 513Combined sources
Beta strandi57 – 593Combined sources
Beta strandi62 – 643Combined sources
Beta strandi71 – 766Combined sources
Beta strandi89 – 913Combined sources
Beta strandi97 – 993Combined sources
Beta strandi113 – 1208Combined sources
Helixi122 – 1243Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi170 – 17910Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi197 – 1993Combined sources
Helixi204 – 2063Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi238 – 2447Combined sources
Beta strandi249 – 2524Combined sources
Beta strandi257 – 2593Combined sources
Beta strandi262 – 2676Combined sources
Beta strandi270 – 2756Combined sources
Beta strandi283 – 2908Combined sources
Turni291 – 2933Combined sources
Beta strandi294 – 2974Combined sources
Helixi302 – 3043Combined sources
Beta strandi306 – 3149Combined sources
Beta strandi317 – 33519Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi353 – 3586Combined sources
Beta strandi361 – 3666Combined sources
Beta strandi374 – 3807Combined sources
Turni381 – 3833Combined sources
Beta strandi384 – 3896Combined sources
Helixi392 – 3943Combined sources
Beta strandi396 – 4049Combined sources
Beta strandi407 – 41610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LAFX-ray2.40A39-421[»]
3O71X-ray1.95B1140-1166[»]
ProteinModelPortaliQ63155.
SMRiQ63155. Positions 419-524, 531-818, 833-1047.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 135110Ig-like C2-type 1Add
BLAST
Domaini139 – 22991Ig-like C2-type 2Add
BLAST
Domaini234 – 32693Ig-like C2-type 3Add
BLAST
Domaini331 – 41686Ig-like C2-type 4Add
BLAST
Domaini431 – 52494Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini530 – 62091Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini625 – 71894Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini728 – 82194Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini846 – 94297Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini947 – 104498Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1252 – 1373122Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. DCC family.Curated
Contains 6 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4221. Eukaryota.
ENOG410Z913. LUCA.
HOGENOMiHOG000230686.
HOVERGENiHBG005455.
InParanoidiQ63155.
KOiK06765.
TreeFamiTF321506.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR033012. DCC.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR010560. Neogenin_C.
[Graphical view]
PANTHERiPTHR10489:SF68. PTHR10489:SF68. 1 hit.
PfamiPF00041. fn3. 6 hits.
PF07679. I-set. 3 hits.
PF13895. Ig_2. 1 hit.
PF06583. Neogenin_C. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 5 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENSLGCVWV PKLAFVLFGA SLLSAHLQVT GFQIKPFTSL HFVSEPSDAV
60 70 80 90 100
TMRGGNVLLN CSAESDRGVP VIKWKKDGLI LALGMDDRKQ QLPNGSLLIQ
110 120 130 140 150
NILHSRHHKP DEGLYQCEAS LGDSGSIISR TAKVMVAGPL RFLSQTESIT
160 170 180 190 200
AFMGDTVLLK CEVIGDPMPT IHWQKNQQDL NPIPGDSRVV VLPSGALQIS
210 220 230 240 250
RLQPGDSGVY RCSARNPAST RTGNEAEVRI LSDPGLHRQL YFLQRPSNVI
260 270 280 290 300
AIEGKDAVLE CCVSGYPPPS FTWLRGEEVI QLRSKKYSLL GGSNLLISNV
310 320 330 340 350
TDDDSGTYTC VVTYKNENIS ASAELTVLVP PWFLNHPSNL YAYESMDIEF
360 370 380 390 400
ECAVSGKPVP TVNWMKNGDV VIPSDYFQIV GGSNLRILGV VKSDEGFYQC
410 420 430 440 450
VAENEAGNAQ SSAQLIVPKP AIPSSSILPS APRDVVPVLV SSRFVRLSWR
460 470 480 490 500
PPAEAKGNIQ TFTVFFSREG DNRERALNTT QPGSLQLTVG NLKPEAMYTF
510 520 530 540 550
RVVAYNEWGP GESSQPIKVA TQPELQVPGP VENLHAVSAS PTSILITWEP
560 570 580 590 600
PAYANGPVQG YRLFCTEVST GKEQNIEVDG LSYKLEGLKK FTEYTLRFLA
610 620 630 640 650
YNRYGPGVST DDITVVTLSD VPSAPPQNVS LEVVNSRSIK VSWLPPPSGT
660 670 680 690 700
QNGFITGYKI RHRKTTRRGE METLEPNNLW YLFTGLEKGS QYSFQVSAMT
710 720 730 740 750
VNGTGPPSNW YTAETPENDL DESQVPDQPS SLHVRPQTNC IIMSWTPPLN
760 770 780 790 800
PNIVVRGYII GYGVGSPYAE TVRVDSKQRY YSIERLESSS HYVISLKAFN
810 820 830 840 850
NAGEGVPLYE SATTRSITDP TDPVDYYPLL DDFPTSGPDV STPMLPPVGV
860 870 880 890 900
QAVALTHEAV RVSWADNSVP KNQKTSDVRL YTVRWRTSFS ASAKYKSEDT
910 920 930 940 950
TSLSYTATGL KPNTMYEFSV MVTKNRRSST WSMTAHATTY EAAPTSAPKD
960 970 980 990 1000
LTVITREGKP RAVIVSWQPP LEANGKITAY ILFYTLDKNI PIDDWIMETI
1010 1020 1030 1040 1050
SGDRLTHQIM DLSLDTMYYF RIQARNAKGV GPLSDPILFR TLKVEHPDKM
1060 1070 1080 1090 1100
ANDQGRHGDG GYWPVDTNLI DRSTLNEPPI GQMHPPHGSV TPQKNSNLLV
1110 1120 1130 1140 1150
ITVVTVGVLT VLVVVIVAVI CTRRSSAQQR KKRATHSASK RKGSQKDLRP
1160 1170 1180 1190 1200
PDLWIHHEEM EMKNIEKPAG TDPAGRGSPI QSCQDLTPVS HSQSESQMGS
1210 1220 1230 1240 1250
KSASHSGQDT EEAGSSMSTL ERSLAARRAT RTKLMIPMEA QSNNPAVVSA
1260 1270 1280 1290 1300
IPVPTLESAQ YPGILPSPTC GYPHPQFTLR PVPFPTLSVD RGFGAGRTVS
1310 1320 1330 1340 1350
EGPTAQQQPM LPPAQPEHPS SEEAPSRTIP TACVRPTHPL RSFANPLLPP
1360 1370 1380 1390 1400
PMSAIEPKVP YTPLLSQPGP TLPKTHVKTA SLGLAGKARS PLLPVSVPTA
1410 1420 1430 1440
PEVSEESHKP TEDPASVYEQ DDLSEQMASL EGLMKQLNAI TGSAF
Length:1,445
Mass (Da):157,941
Last modified:January 1, 1998 - v2
Checksum:i084F625954481988
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68725 mRNA. Translation: AAB41099.1.
CH473971 Genomic DNA. Translation: EDM14792.1.
RefSeqiNP_036973.1. NM_012841.1.
UniGeneiRn.10666.

Genome annotation databases

GeneIDi25311.
KEGGirno:25311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68725 mRNA. Translation: AAB41099.1.
CH473971 Genomic DNA. Translation: EDM14792.1.
RefSeqiNP_036973.1. NM_012841.1.
UniGeneiRn.10666.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LAFX-ray2.40A39-421[»]
3O71X-ray1.95B1140-1166[»]
ProteinModelPortaliQ63155.
SMRiQ63155. Positions 419-524, 531-818, 833-1047.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46811N.
IntActiQ63155. 9 interactions.
STRINGi10116.ENSRNOP00000063072.

PTM databases

iPTMnetiQ63155.
PhosphoSiteiQ63155.
UniCarbKBiQ63155.

Proteomic databases

PaxDbiQ63155.
PRIDEiQ63155.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25311.
KEGGirno:25311.

Organism-specific databases

CTDi1630.
RGDi2492. Dcc.

Phylogenomic databases

eggNOGiKOG4221. Eukaryota.
ENOG410Z913. LUCA.
HOGENOMiHOG000230686.
HOVERGENiHBG005455.
InParanoidiQ63155.
KOiK06765.
TreeFamiTF321506.

Miscellaneous databases

EvolutionaryTraceiQ63155.
NextBioi606123.
PROiQ63155.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR033012. DCC.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR010560. Neogenin_C.
[Graphical view]
PANTHERiPTHR10489:SF68. PTHR10489:SF68. 1 hit.
PfamiPF00041. fn3. 6 hits.
PF07679. I-set. 3 hits.
PF13895. Ig_2. 1 hit.
PF06583. Neogenin_C. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 5 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NTN1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. "Structure of DCC and the prediction of N-terminal horseshoe configuration in other neural receptors."
    Chen Q., Liu J.-H., Wang J.-H.
    Submitted (JAN-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 39-421, DISULFIDE BONDS, GLYCOSYLATION AT ASN-60; ASN-94; ASN-299 AND ASN-318.
  5. "Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase."
    Ma W., Shang Y., Wei Z., Wen W., Wang W., Zhang M.
    Structure 18:1502-1511(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1140-1166 IN COMPLEX WITH MAPK1, PHOSPHORYLATION AT SER-1178; THR-1187 AND SER-1267, MUTAGENESIS OF SER-1178; THR-1187 AND SER-1267.

Entry informationi

Entry nameiDCC_RAT
AccessioniPrimary (citable) accession number: Q63155
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.