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Q61087

- LAMB3_MOUSE

UniProt

Q61087 - LAMB3_MOUSE

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Protein
Laminin subunit beta-3
Gene
Lamb3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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 - Biological processi

  1. brown fat cell differentiation Source: MGI
  2. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196595. Anchoring fibril formation.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Lamb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:99915. Lamb3.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. extracellular region Source: Reactome
  3. laminin-5 complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 11681151Laminin subunit beta-3
PRO_0000017072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi220 – 2201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi250 ↔ 259 By similarity
Disulfide bondi252 ↔ 276 By similarity
Disulfide bondi278 ↔ 287 By similarity
Disulfide bondi290 ↔ 310 By similarity
Disulfide bondi313 ↔ 322 By similarity
Disulfide bondi315 ↔ 340 By similarity
Disulfide bondi343 ↔ 352 By similarity
Disulfide bondi355 ↔ 373 By similarity
Disulfide bondi376 ↔ 389 By similarity
Disulfide bondi378 ↔ 396 By similarity
Disulfide bondi398 ↔ 407 By similarity
Disulfide bondi410 ↔ 425 By similarity
Disulfide bondi428 ↔ 441 By similarity
Disulfide bondi430 ↔ 448 By similarity
Disulfide bondi450 ↔ 459 By similarity
Disulfide bondi462 ↔ 475 By similarity
Disulfide bondi478 ↔ 490 By similarity
Disulfide bondi480 ↔ 497 By similarity
Disulfide bondi499 ↔ 508 By similarity
Disulfide bondi516 ↔ 528 By similarity
Disulfide bondi531 ↔ 543 By similarity
Disulfide bondi533 ↔ 550 By similarity
Disulfide bondi552 ↔ 561 By similarity
Disulfide bondi564 ↔ 575 By similarity
Disulfide bondi578 – 578Interchain Inferred
Disulfide bondi581 – 581Interchain Inferred
Glycosylationi601 – 6011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi806 – 8061N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1167 – 1167Interchain Inferred

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ61087.
PRIDEiQ61087.

PTM databases

PhosphoSiteiQ61087.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

BgeeiQ61087.
CleanExiMM_LAMB3.
GenevestigatoriQ61087.

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

Protein-protein interaction databases

IntActiQ61087. 1 interaction.
MINTiMINT-4100159.

Structurei

3D structure databases

ProteinModelPortaliQ61087.
SMRiQ61087. Positions 20-563.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 249228Laminin N-terminal
Add
BLAST
Domaini250 – 31263Laminin EGF-like 1
Add
BLAST
Domaini313 – 37563Laminin EGF-like 2
Add
BLAST
Domaini376 – 42752Laminin EGF-like 3
Add
BLAST
Domaini428 – 47750Laminin EGF-like 4
Add
BLAST
Domaini478 – 53053Laminin EGF-like 5
Add
BLAST
Domaini531 – 57747Laminin EGF-like 6
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni576 – 781206Domain II
Add
BLAST
Regioni782 – 81231Domain alpha
Add
BLAST
Regioni813 – 1168356Domain I
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili732 – 75423 Reviewed prediction
Add
BLAST
Coiled coili827 – 87953 Reviewed prediction
Add
BLAST
Coiled coili944 – 1129186 Reviewed prediction
Add
BLAST

Domaini

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 similaritiesi

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG289025.
GeneTreeiENSGT00740000115270.
HOGENOMiHOG000113279.
HOVERGENiHBG052302.
InParanoidiQ91V90.
KOiK06244.
OMAiRSQMEED.
OrthoDBiEOG77WWBQ.
TreeFamiTF352481.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. 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]

Sequencei

Sequence statusi: Complete.

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

Q61087-1 [UniParc]FASTAAdd to Basket

« Hide

MTAFFLLWLA LPGFLCAQQA CSRGACYPPV GDLLIGRTQL LRASSTCGLT     50
KPETYCTQYG QWQMKCCKCD SRLPRNYNSH RVENVASSSG PMRWWQSQND 100
VSPVSLQLDL DKRMQLQDIM MDFKGLTPAG MLIERSSDFG KTWRVYQYLA 150
TDCASTFPQV HQGQPKNWQD VRCRPLSQRP NGHLTGGKVQ LNLMDLASAI 200
PASQSKKIQE LGDITNLRVN FTKLAPVPQR GSYPPSAYFA VSQLRLQGSC 250
FCHGHADRCA PNPGGSTTAV QVNNVCVCQH NTAGPNCDRC APFYNNRPWR 300
PAEGQDTHEC QRCDCNGHSE TCHFDPAVFA ASQGTNGGVC DNCRDHTEGK 350
NCERCQLHYF RNRRPSAPIH ETCIPCECDP DGAVQGAPCD RLTGQCVCKE 400
YVQGERCDLC KPGFTGLTFA NPKGCHACDC SILGARKDMP CEEETGRCLC 450
LPNVVGPKCD QCAPSHWKLA SGLGCEPCAC DPRNSLSSQC NQFTGQCPCR 500
EGFGGLTCSS AAIRQCPDQT YGHVATGCRA CDCDFRGTEG PGCDKASGRC 550
LCRPGFTGPR CDQCQRGHCD RYPVCVACHS CFQAYDTDLQ EQARRLHSLR 600
NATEGLWTGT GLEDHGLASR LLDAKSKIEQ IRQILEGTSV TEQDVAQVAN 650
GILSIRRTLQ GLPLDLPLEE EMESFSGDLG NLDRSFSRLL LMYRSKKEQF 700
EKLSSEDPSG AFRMLTMAYE QSSRAAQQVS DSSSLLSQLR DSRREAEGLE 750
RQAGGGGTGG AQLMALRLEM ASLPDLTPTI NKLCGRSRQT ACTPGDCPGE 800
LCPQDNGTAC GSHCRGALPR AKGAFHMAGR VAEQLRNFNT QLQQTRQMIR 850
AAEEAASRVQ ADAQRLETQV STSRLLMEED VQRTRLLIQQ VRGFLTDPDT 900
DAATIQQVSE AVLALWLPTD SATVLRKMKE IQAIAARLPN VDSVLSQTKQ 950
DIARARRLQA EAEQARSRAH AVEGQVDDVV GNLRQGTVAL QEAQDTMQGT 1000
GRSLRLIQER VGEVQQVLVP AERLVKGMKE QMSGFWARMK ELRRQAQEEQ 1050
AQAMQARQLA EGASQQAMNA QEGFKRLKQK YTELKDRLGQ SPVLGEQGNR 1100
ILSIKMEAEE LFGETMEMMD KMKDMESELL RGSQAIMLRS ADLSGLEKRV 1150
EQIRSYINGR VLYYATCK 1168
Length:1,168
Mass (Da):128,900
Last modified:July 27, 2011 - v2
Checksum:i66EB2BE1AA232215
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341L → F in AAA85255. 1 Publication
Sequence conflicti271 – 2711Q → R in AAA85255. 1 Publication
Sequence conflicti284 – 2841G → A in AAA85255. 1 Publication
Sequence conflicti320 – 3201E → L in AAA85255. 1 Publication
Sequence conflicti354 – 3541R → P in AAA85255. 1 Publication
Sequence conflicti361 – 3611R → W in AAA85255. 1 Publication
Sequence conflicti420 – 4201A → D in AAA85255. 1 Publication
Sequence conflicti525 – 5251A → P in AAA85255. 1 Publication
Sequence conflicti542 – 5421G → A in AAA85255. 1 Publication
Sequence conflicti646 – 6461A → P in AAA85255. 1 Publication
Sequence conflicti1079 – 10791Q → P in AAA85255. 1 Publication
Sequence conflicti1115 – 11151T → S in AAA85255. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS15637.1.
RefSeqiNP_001264857.1. NM_001277928.1.
NP_032510.2. NM_008484.2.
XP_006497295.1. XM_006497232.1.
XP_006497296.1. XM_006497233.1.
UniGeneiMm.435441.

Genome annotation databases

EnsembliENSMUST00000016315; ENSMUSP00000016315; ENSMUSG00000026639.
ENSMUST00000159955; ENSMUSP00000123875; ENSMUSG00000026639.
GeneIDi16780.
KEGGimmu:16780.
UCSCiuc007eee.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS15637.1.
RefSeqi NP_001264857.1. NM_001277928.1.
NP_032510.2. NM_008484.2.
XP_006497295.1. XM_006497232.1.
XP_006497296.1. XM_006497233.1.
UniGenei Mm.435441.

3D structure databases

ProteinModelPortali Q61087.
SMRi Q61087. Positions 20-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q61087. 1 interaction.
MINTi MINT-4100159.

PTM databases

PhosphoSitei Q61087.

Proteomic databases

PaxDbi Q61087.
PRIDEi Q61087.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000016315 ; ENSMUSP00000016315 ; ENSMUSG00000026639 .
ENSMUST00000159955 ; ENSMUSP00000123875 ; ENSMUSG00000026639 .
GeneIDi 16780.
KEGGi mmu:16780.
UCSCi uc007eee.1. mouse.

Organism-specific databases

CTDi 3914.
MGIi MGI:99915. Lamb3.

Phylogenomic databases

eggNOGi NOG289025.
GeneTreei ENSGT00740000115270.
HOGENOMi HOG000113279.
HOVERGENi HBG052302.
InParanoidi Q91V90.
KOi K06244.
OMAi RSQMEED.
OrthoDBi EOG77WWBQ.
TreeFami TF352481.

Enzyme and pathway databases

Reactomei REACT_196595. Anchoring fibril formation.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

Miscellaneous databases

ChiTaRSi LAMB3. mouse.
NextBioi 290632.
PROi Q61087.
SOURCEi Search...

Gene expression databases

Bgeei Q61087.
CleanExi MM_LAMB3.
Genevestigatori Q61087.

Family and domain databases

InterProi IPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiLAMB3_MOUSE
AccessioniPrimary (citable) accession number: Q61087
Secondary accession number(s): Q91V90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 121 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi