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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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 11681151Laminin subunit beta-3PRO_0000017072Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61087.
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).By similarity

Protein-protein interaction databases

IntActiQ61087. 1 interaction.
MINTiMINT-4100159.

Structurei

3D structure databases

ProteinModelPortaliQ61087.
SMRiQ61087. Positions 20-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni576 – 781206Domain IIAdd
BLAST
Regioni782 – 81231Domain alphaAdd
BLAST
Regioni813 – 1168356Domain IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili732 – 75423Sequence AnalysisAdd
BLAST
Coiled coili827 – 87953Sequence AnalysisAdd
BLAST
Coiled coili944 – 1129186Sequence AnalysisAdd
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

Contains 6 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG289025.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000113279.
HOVERGENiHBG052302.
InParanoidiQ61087.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTAFFLLWLA LPGFLCAQQA CSRGACYPPV GDLLIGRTQL LRASSTCGLT
60 70 80 90 100
KPETYCTQYG QWQMKCCKCD SRLPRNYNSH RVENVASSSG PMRWWQSQND
110 120 130 140 150
VSPVSLQLDL DKRMQLQDIM MDFKGLTPAG MLIERSSDFG KTWRVYQYLA
160 170 180 190 200
TDCASTFPQV HQGQPKNWQD VRCRPLSQRP NGHLTGGKVQ LNLMDLASAI
210 220 230 240 250
PASQSKKIQE LGDITNLRVN FTKLAPVPQR GSYPPSAYFA VSQLRLQGSC
260 270 280 290 300
FCHGHADRCA PNPGGSTTAV QVNNVCVCQH NTAGPNCDRC APFYNNRPWR
310 320 330 340 350
PAEGQDTHEC QRCDCNGHSE TCHFDPAVFA ASQGTNGGVC DNCRDHTEGK
360 370 380 390 400
NCERCQLHYF RNRRPSAPIH ETCIPCECDP DGAVQGAPCD RLTGQCVCKE
410 420 430 440 450
YVQGERCDLC KPGFTGLTFA NPKGCHACDC SILGARKDMP CEEETGRCLC
460 470 480 490 500
LPNVVGPKCD QCAPSHWKLA SGLGCEPCAC DPRNSLSSQC NQFTGQCPCR
510 520 530 540 550
EGFGGLTCSS AAIRQCPDQT YGHVATGCRA CDCDFRGTEG PGCDKASGRC
560 570 580 590 600
LCRPGFTGPR CDQCQRGHCD RYPVCVACHS CFQAYDTDLQ EQARRLHSLR
610 620 630 640 650
NATEGLWTGT GLEDHGLASR LLDAKSKIEQ IRQILEGTSV TEQDVAQVAN
660 670 680 690 700
GILSIRRTLQ GLPLDLPLEE EMESFSGDLG NLDRSFSRLL LMYRSKKEQF
710 720 730 740 750
EKLSSEDPSG AFRMLTMAYE QSSRAAQQVS DSSSLLSQLR DSRREAEGLE
760 770 780 790 800
RQAGGGGTGG AQLMALRLEM ASLPDLTPTI NKLCGRSRQT ACTPGDCPGE
810 820 830 840 850
LCPQDNGTAC GSHCRGALPR AKGAFHMAGR VAEQLRNFNT QLQQTRQMIR
860 870 880 890 900
AAEEAASRVQ ADAQRLETQV STSRLLMEED VQRTRLLIQQ VRGFLTDPDT
910 920 930 940 950
DAATIQQVSE AVLALWLPTD SATVLRKMKE IQAIAARLPN VDSVLSQTKQ
960 970 980 990 1000
DIARARRLQA EAEQARSRAH AVEGQVDDVV GNLRQGTVAL QEAQDTMQGT
1010 1020 1030 1040 1050
GRSLRLIQER VGEVQQVLVP AERLVKGMKE QMSGFWARMK ELRRQAQEEQ
1060 1070 1080 1090 1100
AQAMQARQLA EGASQQAMNA QEGFKRLKQK YTELKDRLGQ SPVLGEQGNR
1110 1120 1130 1140 1150
ILSIKMEAEE LFGETMEMMD KMKDMESELL RGSQAIMLRS ADLSGLEKRV
1160
EQIRSYINGR VLYYATCK
Length:1,168
Mass (Da):128,900
Last modified:July 27, 2011 - v2
Checksum:i66EB2BE1AA232215
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341L → F in AAA85255. (PubMed:7898049)Curated
Sequence conflicti271 – 2711Q → R in AAA85255. (PubMed:7898049)Curated
Sequence conflicti284 – 2841G → A in AAA85255. (PubMed:7898049)Curated
Sequence conflicti320 – 3201E → L in AAA85255. (PubMed:7898049)Curated
Sequence conflicti354 – 3541R → P in AAA85255. (PubMed:7898049)Curated
Sequence conflicti361 – 3611R → W in AAA85255. (PubMed:7898049)Curated
Sequence conflicti420 – 4201A → D in AAA85255. (PubMed:7898049)Curated
Sequence conflicti525 – 5251A → P in AAA85255. (PubMed:7898049)Curated
Sequence conflicti542 – 5421G → A in AAA85255. (PubMed:7898049)Curated
Sequence conflicti646 – 6461A → P in AAA85255. (PubMed:7898049)Curated
Sequence conflicti1079 – 10791Q → P in AAA85255. (PubMed:7898049)Curated
Sequence conflicti1115 – 11151T → S in AAA85255. (PubMed:7898049)Curated

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

MaxQBi Q61087.
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 ENSGT00760000118860.
HOGENOMi HOG000113279.
HOVERGENi HBG052302.
InParanoidi Q61087.
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: October 29, 2014
This is version 123 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