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Q61087 (LAMB3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit beta-3
Alternative name(s):
Epiligrin subunit bata
Kalinin B1 chain
Kalinin subunit beta
Laminin-5 subunit beta
Nicein subunit beta
Gene names
Name:Lamb3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1168 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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. Beta-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1 By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix › basement membrane.

Tissue specificity

Found in the basement membranes (major component).

Domain

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

Domain VI is globular.

Sequence similarities

Contains 6 laminin EGF-like domains.

Contains 1 laminin N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 11681151Laminin subunit beta-3
PRO_0000017072

Regions

Domain22 – 249228Laminin N-terminal
Domain250 – 31263Laminin EGF-like 1
Domain313 – 37563Laminin EGF-like 2
Domain376 – 42752Laminin EGF-like 3
Domain428 – 47750Laminin EGF-like 4
Domain478 – 53053Laminin EGF-like 5
Domain531 – 57747Laminin EGF-like 6
Region576 – 781206Domain II
Region782 – 81231Domain alpha
Region813 – 1168356Domain I
Coiled coil732 – 75423 Potential
Coiled coil827 – 87953 Potential
Coiled coil944 – 1129186 Potential

Amino acid modifications

Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation6011N-linked (GlcNAc...) Potential
Glycosylation8061N-linked (GlcNAc...) Potential
Disulfide bond250 ↔ 259 By similarity
Disulfide bond252 ↔ 276 By similarity
Disulfide bond278 ↔ 287 By similarity
Disulfide bond290 ↔ 310 By similarity
Disulfide bond313 ↔ 322 By similarity
Disulfide bond315 ↔ 340 By similarity
Disulfide bond343 ↔ 352 By similarity
Disulfide bond355 ↔ 373 By similarity
Disulfide bond376 ↔ 389 By similarity
Disulfide bond378 ↔ 396 By similarity
Disulfide bond398 ↔ 407 By similarity
Disulfide bond410 ↔ 425 By similarity
Disulfide bond428 ↔ 441 By similarity
Disulfide bond430 ↔ 448 By similarity
Disulfide bond450 ↔ 459 By similarity
Disulfide bond462 ↔ 475 By similarity
Disulfide bond478 ↔ 490 By similarity
Disulfide bond480 ↔ 497 By similarity
Disulfide bond499 ↔ 508 By similarity
Disulfide bond516 ↔ 528 By similarity
Disulfide bond531 ↔ 543 By similarity
Disulfide bond533 ↔ 550 By similarity
Disulfide bond552 ↔ 561 By similarity
Disulfide bond564 ↔ 575 By similarity
Disulfide bond578Interchain Probable
Disulfide bond581Interchain Probable
Disulfide bond1167Interchain Probable

Experimental info

Sequence conflict341L → F in AAA85255. Ref.1
Sequence conflict2711Q → R in AAA85255. Ref.1
Sequence conflict2841G → A in AAA85255. Ref.1
Sequence conflict3201E → L in AAA85255. Ref.1
Sequence conflict3541R → P in AAA85255. Ref.1
Sequence conflict3611R → W in AAA85255. Ref.1
Sequence conflict4201A → D in AAA85255. Ref.1
Sequence conflict5251A → P in AAA85255. Ref.1
Sequence conflict5421G → A in AAA85255. Ref.1
Sequence conflict6461A → P in AAA85255. Ref.1
Sequence conflict10791Q → P in AAA85255. Ref.1
Sequence conflict11151T → S in AAA85255. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61087 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 66EB2BE1AA232215

FASTA1,168128,900
        10         20         30         40         50         60 
MTAFFLLWLA LPGFLCAQQA CSRGACYPPV GDLLIGRTQL LRASSTCGLT KPETYCTQYG 

        70         80         90        100        110        120 
QWQMKCCKCD SRLPRNYNSH RVENVASSSG PMRWWQSQND VSPVSLQLDL DKRMQLQDIM 

       130        140        150        160        170        180 
MDFKGLTPAG MLIERSSDFG KTWRVYQYLA TDCASTFPQV HQGQPKNWQD VRCRPLSQRP 

       190        200        210        220        230        240 
NGHLTGGKVQ LNLMDLASAI PASQSKKIQE LGDITNLRVN FTKLAPVPQR GSYPPSAYFA 

       250        260        270        280        290        300 
VSQLRLQGSC FCHGHADRCA PNPGGSTTAV QVNNVCVCQH NTAGPNCDRC APFYNNRPWR 

       310        320        330        340        350        360 
PAEGQDTHEC QRCDCNGHSE TCHFDPAVFA ASQGTNGGVC DNCRDHTEGK NCERCQLHYF 

       370        380        390        400        410        420 
RNRRPSAPIH ETCIPCECDP DGAVQGAPCD RLTGQCVCKE YVQGERCDLC KPGFTGLTFA 

       430        440        450        460        470        480 
NPKGCHACDC SILGARKDMP CEEETGRCLC LPNVVGPKCD QCAPSHWKLA SGLGCEPCAC 

       490        500        510        520        530        540 
DPRNSLSSQC NQFTGQCPCR EGFGGLTCSS AAIRQCPDQT YGHVATGCRA CDCDFRGTEG 

       550        560        570        580        590        600 
PGCDKASGRC LCRPGFTGPR CDQCQRGHCD RYPVCVACHS CFQAYDTDLQ EQARRLHSLR 

       610        620        630        640        650        660 
NATEGLWTGT GLEDHGLASR LLDAKSKIEQ IRQILEGTSV TEQDVAQVAN GILSIRRTLQ 

       670        680        690        700        710        720 
GLPLDLPLEE EMESFSGDLG NLDRSFSRLL LMYRSKKEQF EKLSSEDPSG AFRMLTMAYE 

       730        740        750        760        770        780 
QSSRAAQQVS DSSSLLSQLR DSRREAEGLE RQAGGGGTGG AQLMALRLEM ASLPDLTPTI 

       790        800        810        820        830        840 
NKLCGRSRQT ACTPGDCPGE LCPQDNGTAC GSHCRGALPR AKGAFHMAGR VAEQLRNFNT 

       850        860        870        880        890        900 
QLQQTRQMIR AAEEAASRVQ ADAQRLETQV STSRLLMEED VQRTRLLIQQ VRGFLTDPDT 

       910        920        930        940        950        960 
DAATIQQVSE AVLALWLPTD SATVLRKMKE IQAIAARLPN VDSVLSQTKQ DIARARRLQA 

       970        980        990       1000       1010       1020 
EAEQARSRAH AVEGQVDDVV GNLRQGTVAL QEAQDTMQGT GRSLRLIQER VGEVQQVLVP 

      1030       1040       1050       1060       1070       1080 
AERLVKGMKE QMSGFWARMK ELRRQAQEEQ AQAMQARQLA EGASQQAMNA QEGFKRLKQK 

      1090       1100       1110       1120       1130       1140 
YTELKDRLGQ SPVLGEQGNR ILSIKMEAEE LFGETMEMMD KMKDMESELL RGSQAIMLRS 

      1150       1160 
ADLSGLEKRV EQIRSYINGR VLYYATCK

« Hide

References

« Hide 'large scale' references
[1]"Mouse kalinin B1 (laminin beta 3 chain): cloning and tissue distribution."
Utani A., Kopp J.B., Kozak C.A., Matsuki Y., Amizuka N., Sugiyama S., Yamada Y.
Lab. Invest. 72:300-310(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FVB.
Tissue: Lung.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U43298 mRNA. Translation: AAA85255.1.
AK155769 mRNA. Translation: BAE33428.1.
CH466555 Genomic DNA. Translation: EDL12945.1.
CH466555 Genomic DNA. Translation: EDL12946.1.
BC008516 mRNA. Translation: AAH08516.1.
IPIIPI00117093.
RefSeqNP_032510.2. NM_008484.2.
UniGeneMm.435441.

3D structure databases

ProteinModelPortalQ61087.
SMRQ61087. Positions 20-563.
ModBaseSearch...

PTM databases

PhosphoSiteQ61087.

Proteomic databases

PaxDbQ61087.
PRIDEQ61087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016315; ENSMUSP00000016315; ENSMUSG00000026639.
ENSMUST00000159955; ENSMUSP00000123875; ENSMUSG00000026639.
GeneID16780.
KEGGmmu:16780.

Organism-specific databases

CTD3914.
MGIMGI:99915. Lamb3.

Phylogenomic databases

eggNOGNOG289025.
GeneTreeENSGT00620000087753.
HOGENOMHOG000113279.
HOVERGENHBG052302.
InParanoidQ91V90.
KOK06244.
OMARSQMEED.
OrthoDBEOG4JDH5Z.

Gene expression databases

BgeeQ61087.
CleanExMM_LAMB3.
GenevestigatorQ61087.
GermOnlineENSMUSG00000026639. Mus musculus.

Family and domain databases

InterProIPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 4 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMB3. mouse.
NextBio290632.
SOURCESearch...

Entry information

Entry nameLAMB3_MOUSE
AccessionPrimary (citable) accession number: Q61087
Secondary accession number(s): Q91V90
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents