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Protein

Laminin subunit gamma-1

Gene

Lamc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.

GO - Molecular functioni

  • extracellular matrix structural constituent Source: HGNC
  • glycosphingolipid binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-373760. L1CAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-1
Alternative name(s):
Laminin B2 chain
Laminin-1 subunit gamma
Laminin-10 subunit gamma
Laminin-11 subunit gamma
Laminin-2 subunit gamma
Laminin-3 subunit gamma
Laminin-4 subunit gamma
Laminin-6 subunit gamma
Laminin-7 subunit gamma
Laminin-8 subunit gamma
Laminin-9 subunit gamma
S-laminin subunit gamma
Short name:
S-LAM gamma
Gene namesi
Name:Lamc1
Synonyms:Lamb-2, Lamc-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:99914. Lamc1.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: MGI
  • basement membrane Source: HGNC
  • extracellular exosome Source: MGI
  • extracellular matrix Source: MGI
  • extracellular region Source: Reactome
  • laminin-10 complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Add BLAST33
ChainiPRO_000001707534 – 1607Laminin subunit gamma-1Add BLAST1574

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi58N-linked (GlcNAc...)Sequence analysis1
Glycosylationi132N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi284 ↔ 293PROSITE-ProRule annotation
Disulfide bondi286 ↔ 303PROSITE-ProRule annotation
Disulfide bondi305 ↔ 314PROSITE-ProRule annotation
Disulfide bondi340 ↔ 349PROSITE-ProRule annotation
Disulfide bondi342 ↔ 365PROSITE-ProRule annotation
Disulfide bondi368 ↔ 377PROSITE-ProRule annotation
Disulfide bondi380 ↔ 393PROSITE-ProRule annotation
Disulfide bondi396 ↔ 408PROSITE-ProRule annotation
Disulfide bondi398 ↔ 414PROSITE-ProRule annotation
Disulfide bondi416 ↔ 425PROSITE-ProRule annotation
Disulfide bondi428 ↔ 440PROSITE-ProRule annotation
Disulfide bondi443 ↔ 454PROSITE-ProRule annotation
Disulfide bondi445 ↔ 461PROSITE-ProRule annotation
Disulfide bondi463 ↔ 472PROSITE-ProRule annotation
Disulfide bondi475 ↔ 490PROSITE-ProRule annotation
Glycosylationi574N-linked (GlcNAc...)Sequence analysis1
Glycosylationi648N-linked (GlcNAc...)1 Publication1
Disulfide bondi722 ↔ 731PROSITE-ProRule annotation
Disulfide bondi724 ↔ 738PROSITE-ProRule annotation
Disulfide bondi740 ↔ 749PROSITE-ProRule annotation
Disulfide bondi752 ↔ 768PROSITE-ProRule annotation
Disulfide bondi771 ↔ 779
Disulfide bondi773 ↔ 790
Disulfide bondi793 ↔ 802
Disulfide bondi805 ↔ 823
Disulfide bondi826 ↔ 840
Disulfide bondi828 ↔ 847
Disulfide bondi850 ↔ 859
Disulfide bondi862 ↔ 879
Disulfide bondi882 ↔ 896
Disulfide bondi884 ↔ 903
Disulfide bondi905 ↔ 914
Disulfide bondi917 ↔ 930
Disulfide bondi933 ↔ 945PROSITE-ProRule annotation
Disulfide bondi935 ↔ 952PROSITE-ProRule annotation
Disulfide bondi954 ↔ 963PROSITE-ProRule annotation
Disulfide bondi966 ↔ 978PROSITE-ProRule annotation
Disulfide bondi981 ↔ 993PROSITE-ProRule annotation
Disulfide bondi983 ↔ 999PROSITE-ProRule annotation
Disulfide bondi1001 ↔ 1010PROSITE-ProRule annotation
Disulfide bondi1013 ↔ 1026PROSITE-ProRule annotation
Glycosylationi1020N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1029InterchainCurated
Disulfide bondi1032InterchainCurated
Glycosylationi1105N-linked (GlcNAc...)1 Publication1
Modified residuei1147PhosphoserineBy similarity1
Glycosylationi1159N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1173N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1203N-linked (GlcNAc...)1 Publication1
Glycosylationi1221N-linked (GlcNAc...)1 Publication1
Glycosylationi1239N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1378N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1393N-linked (GlcNAc...)1 Publication1
Glycosylationi1437N-linked (GlcNAc...)Sequence analysis1
Modified residuei1491PhosphoserineBy similarity1
Disulfide bondi1598Interchain (with beta-1 chain)

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP02468.
MaxQBiP02468.
PaxDbiP02468.
PeptideAtlasiP02468.
PRIDEiP02468.

PTM databases

iPTMnetiP02468.
PhosphoSitePlusiP02468.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

CleanExiMM_LAMC1.

Interactioni

Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 (laminin-521).

Binary interactionsi

WithEntry#Exp.IntActNotes
Lamb1P024694EBI-7059830,EBI-6662997
Nid1P104933EBI-7059830,EBI-1032117

Protein-protein interaction databases

DIPiDIP-41793N.
IntActiP02468. 5 interactors.
MINTiMINT-1031545.
STRINGi10090.ENSMUSP00000027752.

Structurei

Secondary structure

11607
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni55 – 58Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi72 – 75Combined sources4
Beta strandi87 – 90Combined sources4
Beta strandi92 – 94Combined sources3
Turni95 – 97Combined sources3
Helixi101 – 104Combined sources4
Beta strandi110 – 112Combined sources3
Helixi121 – 123Combined sources3
Beta strandi126 – 128Combined sources3
Beta strandi131 – 153Combined sources23
Beta strandi156 – 168Combined sources13
Beta strandi171 – 177Combined sources7
Helixi180 – 184Combined sources5
Beta strandi202 – 205Combined sources4
Beta strandi212 – 214Combined sources3
Beta strandi216 – 221Combined sources6
Turni222 – 225Combined sources4
Helixi229 – 234Combined sources6
Helixi236 – 241Combined sources6
Beta strandi243 – 253Combined sources11
Helixi259 – 261Combined sources3
Helixi265 – 268Combined sources4
Beta strandi274 – 284Combined sources11
Beta strandi293 – 295Combined sources3
Beta strandi301 – 303Combined sources3
Beta strandi309 – 311Combined sources3
Helixi342 – 344Combined sources3
Beta strandi349 – 351Combined sources3
Helixi353 – 358Combined sources6
Beta strandi363 – 365Combined sources3
Turni369 – 371Combined sources3
Beta strandi372 – 374Combined sources3
Beta strandi382 – 385Combined sources4
Beta strandi779 – 781Combined sources3
Beta strandi783 – 785Combined sources3
Beta strandi788 – 790Combined sources3
Beta strandi797 – 799Combined sources3
Beta strandi809 – 812Combined sources4
Beta strandi816 – 819Combined sources4
Beta strandi821 – 825Combined sources5
Beta strandi834 – 837Combined sources4
Turni842 – 844Combined sources3
Beta strandi846 – 849Combined sources4
Turni856 – 859Combined sources4
Beta strandi866 – 868Combined sources3
Helixi875 – 877Combined sources3
Beta strandi878 – 881Combined sources4
Turni886 – 888Combined sources3
Helixi890 – 892Combined sources3
Turni898 – 900Combined sources3
Beta strandi909 – 911Combined sources3
Helixi924 – 926Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KLOX-ray2.10A771-932[»]
1NPEX-ray2.30B769-932[»]
1TLENMR-A824-881[»]
4AQTX-ray3.20A33-395[»]
ProteinModelPortaliP02468.
SMRiP02468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02468.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 283Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini284 – 339Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini340 – 395Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini396 – 442Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Domaini443 – 492Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST50
Domaini493 – 502Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini512 – 687Laminin IV type APROSITE-ProRule annotationAdd BLAST176
Domaini688 – 721Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST34
Domaini722 – 770Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST49
Domaini771 – 825Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST55
Domaini826 – 881Laminin EGF-like 8; nidogen-bindingPROSITE-ProRule annotationAdd BLAST56
Domaini882 – 932Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST51
Domaini933 – 980Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST48
Domaini981 – 1028Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST48

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1029 – 1607Domain II and IAdd BLAST579

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1034 – 1594Sequence analysisAdd BLAST561

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI and IV are globular.

Sequence similaritiesi

Contains 11 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiP02468.
PhylomeDBiP02468.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 9 hits.
SM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP
60 70 80 90 100
EFVNAAFNVT VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG
110 120 130 140 150
AAFLTDYNNQ ADTTWWQSQT MLAGVQYPNS INLTLHLGKA FDITYVRLKF
160 170 180 190 200
HTSRPESFAI YKRTREDGPW IPYQYYSGSC ENTYSKANRG FIRTGGDEQQ
210 220 230 240 250
ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE WVTATDIRVT
260 270 280 290 300
LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK
310 320 330 340 350
LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY
360 370 380 390 400
FDPELYRSTG HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP
410 420 430 440 450
VGSLSTQCDS YGRCSCKPGV MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS
460 470 480 490 500
TDECNVETGR CVCKDNVEGF NCERCKPGFF NLESSNPKGC TPCFCFGHSS
510 520 530 540 550
VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS DRQDIAVISD
560 570 580 590 600
SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL
610 620 630 640 650
RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT
660 670 680 690 700
SIKIRGTYSE RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE
710 720 730 740 750
TCLPGYRRET PSLGPYSPCV LCTCNGHSET CDPETGVCDC RDNTAGPHCE
760 770 780 790 800
KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA IVPKTKEVVC THCPTGTAGK
810 820 830 840 850
RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC NRLTGECLKC
860 870 880 890 900
IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT
910 920 930 940 950
GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG
960 970 980 990 1000
QCECQPGITG QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE
1010 1020 1030 1040 1050
CREGFVGNRC DQCEENYFYN RSWPGCQECP ACYRLVKDKA AEHRVKLQEL
1060 1070 1080 1090 1100
ESLIANLGTG DDMVTDQAFE DRLKEAEREV TDLLREAQEV KDVDQNLMDR
1110 1120 1130 1140 1150
LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE QLIEIASREL
1160 1170 1180 1190 1200
EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK
1210 1220 1230 1240 1250
TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR
1260 1270 1280 1290 1300
VHEEAKRAGD KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ
1310 1320 1330 1340 1350
KLKDYEDLRE DMRGKEHEVK NLLEKGKAEQ QTADQLLARA DAAKALAEEA
1360 1370 1380 1390 1400
AKKGRSTLQE ANDILNNLKD FDRRVNDNKT AAEEALRRIP AINRTIAEAN
1410 1420 1430 1440 1450
EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS TKADAERTFG
1460 1470 1480 1490 1500
EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN
1510 1520 1530 1540 1550
ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS
1560 1570 1580 1590 1600
DLDRKVSDLE SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN

TPSIEKP
Length:1,607
Mass (Da):177,298
Last modified:July 1, 1989 - v2
Checksum:i81B7B08E4869F242
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti216G → A in AAA39409 (PubMed:2836421).Curated1
Sequence conflicti260E → D (PubMed:3167041).Curated1
Sequence conflicti337S → C in AAA39408 (PubMed:3167041).Curated1
Sequence conflicti447 – 448LR → PS in AAA39408 (PubMed:3167041).Curated2
Sequence conflicti544D → Y in AAA39408 (PubMed:3167041).Curated1
Sequence conflicti662T → S in AAA39408 (PubMed:3167041).Curated1
Sequence conflicti886Missing in AAA39408 (PubMed:3167041).Curated1
Sequence conflicti1158Missing in AAA39408 (PubMed:3167041).Curated1
Sequence conflicti1434V → A in AAA39408 (PubMed:3167041).Curated1
Sequence conflicti1475R → K in CAA28838 (PubMed:6209134).Curated1
Sequence conflicti1576D → N in CAA28838 (PubMed:6209134).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05211 mRNA. Translation: CAA28838.1.
J03484 mRNA. Translation: AAA39405.1.
J02930 mRNA. Translation: AAA39408.1.
J03749 Genomic DNA. Translation: AAA39409.1.
CCDSiCCDS15370.1.
PIRiA28469. MMMSB2.
S55783.
UniGeneiMm.1249.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05211 mRNA. Translation: CAA28838.1.
J03484 mRNA. Translation: AAA39405.1.
J02930 mRNA. Translation: AAA39408.1.
J03749 Genomic DNA. Translation: AAA39409.1.
CCDSiCCDS15370.1.
PIRiA28469. MMMSB2.
S55783.
UniGeneiMm.1249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KLOX-ray2.10A771-932[»]
1NPEX-ray2.30B769-932[»]
1TLENMR-A824-881[»]
4AQTX-ray3.20A33-395[»]
ProteinModelPortaliP02468.
SMRiP02468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41793N.
IntActiP02468. 5 interactors.
MINTiMINT-1031545.
STRINGi10090.ENSMUSP00000027752.

PTM databases

iPTMnetiP02468.
PhosphoSitePlusiP02468.

Proteomic databases

EPDiP02468.
MaxQBiP02468.
PaxDbiP02468.
PeptideAtlasiP02468.
PRIDEiP02468.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:99914. Lamc1.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiP02468.
PhylomeDBiP02468.

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-373760. L1CAM interactions.

Miscellaneous databases

ChiTaRSiLamc1. mouse.
EvolutionaryTraceiP02468.
PROiP02468.
SOURCEiSearch...

Gene expression databases

CleanExiMM_LAMC1.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 9 hits.
SM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMC1_MOUSE
AccessioniPrimary (citable) accession number: P02468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 168 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.