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Q61789 (LAMA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit alpha-3
Alternative name(s):
Epiligrin subunit alpha
Kalinin subunit alpha
Laminin-5 subunit alpha
Laminin-6 subunit alpha
Laminin-7 subunit alpha
Nicein subunit alpha
Gene names
Name:Lama3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes By similarity.

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. Alpha-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

Basal membrane of the upper alimentary tract and urinary and nasal epithelia, salivary glands and teeth (both variants). Isoform A is predominantly expressed in skin, hair follicles and developing neurons of the trigeminal ganglion. Isoform B was found in bronchi, alveoli, stomach, intestinal crypts, whisker pads, CNS, telencephalic neuroectoderm, thalamus, Rathke pouch and periventricular subependymal germinal layer.

Domain

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

Domains IV and G are globular.

Sequence similarities

Contains 15 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence CAA58837.1 differs from that shown. Reason: Frameshift at several positions.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: Q61789-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: Q61789-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1619: Missing.
     1620-1662: FTETQRLTLG...CPPDYTGDSC → MLPAVRWSAW...QASYMELRPS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.4
Chain32 – 33303299Laminin subunit alpha-3
PRO_0000017059

Regions

Domain40 – 295256Laminin N-terminal
Domain296 – 35055Laminin EGF-like 1
Domain353 – 42068Laminin EGF-like 2
Domain423 – 46442Laminin EGF-like 3
Domain488 – 53043Laminin EGF-like 4
Domain533 – 57644Laminin EGF-like 5
Domain582 – 62544Laminin EGF-like 6
Domain628 – 67851Laminin EGF-like 7
Domain681 – 72545Laminin EGF-like 8
Domain1309 – 135244Laminin EGF-like 9
Domain1353 – 140149Laminin EGF-like 10
Domain1402 – 145251Laminin EGF-like 11
Domain1453 – 146210Laminin EGF-like 12; first part
Domain1466 – 1650185Laminin IV type A
Domain1651 – 168333Laminin EGF-like 12; second part
Domain1684 – 173047Laminin EGF-like 13
Domain1731 – 178353Laminin EGF-like 14
Domain1784 – 181835Laminin EGF-like 15; truncated
Domain2386 – 2587202Laminin G-like 1
Domain2594 – 2756163Laminin G-like 2
Domain2763 – 2923161Laminin G-like 3
Domain2983 – 3147165Laminin G-like 4
Domain3154 – 3327174Laminin G-like 5
Region295 – 725431Domain V
Region793 – 1262470Domain IV 1 (domain IV B)
Region1263 – 1462200Domain III B
Region1651 – 1818168Domain III A
Region1819 – 2385567Domain II and I
Coiled coil1851 – 1980130 Potential
Coiled coil2012 – 205746 Potential
Coiled coil2088 – 216578 Potential
Coiled coil2211 – 223828 Potential
Coiled coil2318 – 238366 Potential
Motif2274 – 22763Cell attachment site Potential

Amino acid modifications

Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation13541N-linked (GlcNAc...) Potential
Glycosylation16731N-linked (GlcNAc...) Potential
Glycosylation21591N-linked (GlcNAc...) Potential
Glycosylation22611N-linked (GlcNAc...) Potential
Glycosylation23321N-linked (GlcNAc...) Potential
Glycosylation23611N-linked (GlcNAc...) Potential
Glycosylation24981N-linked (GlcNAc...) Potential
Glycosylation25801N-linked (GlcNAc...) Potential
Glycosylation27471N-linked (GlcNAc...) Potential
Glycosylation30941N-linked (GlcNAc...) Potential
Glycosylation32701N-linked (GlcNAc...) Potential
Disulfide bond296 ↔ 305 By similarity
Disulfide bond298 ↔ 316 By similarity
Disulfide bond318 ↔ 327 By similarity
Disulfide bond330 ↔ 350 By similarity
Disulfide bond353 ↔ 362 By similarity
Disulfide bond355 ↔ 387 By similarity
Disulfide bond390 ↔ 399 By similarity
Disulfide bond402 ↔ 420 By similarity
Disulfide bond423 ↔ 433 By similarity
Disulfide bond425 ↔ 440 By similarity
Disulfide bond442 ↔ 451 By similarity
Disulfide bond454 ↔ 464 By similarity
Disulfide bond488 ↔ 500 By similarity
Disulfide bond490 ↔ 506 By similarity
Disulfide bond508 ↔ 517 By similarity
Disulfide bond520 ↔ 530 By similarity
Disulfide bond533 ↔ 545 By similarity
Disulfide bond535 ↔ 552 By similarity
Disulfide bond554 ↔ 563 By similarity
Disulfide bond566 ↔ 583 By similarity
Disulfide bond628 ↔ 642 By similarity
Disulfide bond630 ↔ 649 By similarity
Disulfide bond651 ↔ 660 By similarity
Disulfide bond663 ↔ 678 By similarity
Disulfide bond681 ↔ 693 By similarity
Disulfide bond683 ↔ 700 By similarity
Disulfide bond702 ↔ 711 By similarity
Disulfide bond1309 ↔ 1316 By similarity
Disulfide bond1311 ↔ 1323 By similarity
Disulfide bond1325 ↔ 1334 By similarity
Disulfide bond1337 ↔ 1350 By similarity
Disulfide bond1353 ↔ 1368 By similarity
Disulfide bond1355 ↔ 1375 By similarity
Disulfide bond1377 ↔ 1386 By similarity
Disulfide bond1389 ↔ 1399 By similarity
Disulfide bond1402 ↔ 1414 By similarity
Disulfide bond1404 ↔ 1421 By similarity
Disulfide bond1423 ↔ 1432 By similarity
Disulfide bond1435 ↔ 1450 By similarity
Disulfide bond1684 ↔ 1693 By similarity
Disulfide bond1686 ↔ 1700 By similarity
Disulfide bond1703 ↔ 1712 By similarity
Disulfide bond1715 ↔ 1728 By similarity
Disulfide bond1731 ↔ 1743 By similarity
Disulfide bond1733 ↔ 1752 By similarity
Disulfide bond1754 ↔ 1763 By similarity
Disulfide bond1766 ↔ 1781 By similarity
Disulfide bond1819Interchain Probable
Disulfide bond1822Interchain Probable
Disulfide bond2557 ↔ 2587 By similarity
Disulfide bond2733 ↔ 2756 By similarity
Disulfide bond2891 ↔ 2923 By similarity
Disulfide bond3124 ↔ 3147 By similarity
Disulfide bond3299 ↔ 3327 By similarity

Natural variations

Alternative sequence1 – 16191619Missing in isoform A.
VSP_003038
Alternative sequence1620 – 166243FTETQ…TGDSC → MLPAVRWSAWSTGWLWIFGA ALGQCLGYGSEQQRVAFLQR PSQNHLQASYMELRPS in isoform A.
VSP_003039

Experimental info

Sequence conflict9821A → R in CAA58837. Ref.1
Sequence conflict11501W → R in CAA58837. Ref.1
Sequence conflict12241E → K in CAA58837. Ref.1
Sequence conflict12721G → GH in CAA58837. Ref.1
Sequence conflict12911R → S in CAA58837. Ref.1
Sequence conflict13981E → K in CAA58837. Ref.1
Sequence conflict14661H → R in CAA58837. Ref.1
Sequence conflict14791R → V in CAA58837. Ref.1
Sequence conflict14881V → F in CAA58837. Ref.1
Sequence conflict1527 – 15282SS → II in CAA58837. Ref.1
Sequence conflict16081S → P in CAA58837. Ref.1
Sequence conflict1983 – 19842KK → QN in CAA58836. Ref.1
Sequence conflict1983 – 19842KK → QN in CAA58837. Ref.1
Sequence conflict1983 – 19842KK → QN in AAA68091. Ref.6
Sequence conflict19871Q → G in CAA58836. Ref.1
Sequence conflict19871Q → G in CAA58837. Ref.1
Sequence conflict19871Q → G in AAA68091. Ref.6
Sequence conflict24631R → G in CAA58836. Ref.1
Sequence conflict24631R → G in CAA58837. Ref.1
Sequence conflict24631R → G in AAA68091. Ref.6
Sequence conflict24881F → S in CAA58836. Ref.1
Sequence conflict24881F → S in CAA58837. Ref.1
Sequence conflict24881F → S in AAA68091. Ref.6
Sequence conflict2617 – 26204NFMQ → KLSW in CAA58836. Ref.1
Sequence conflict2617 – 26204NFMQ → KLSW in CAA58837. Ref.1
Sequence conflict2724 – 27252NI → PL in CAA58836. Ref.1
Sequence conflict2724 – 27252NI → PL in CAA58837. Ref.1
Sequence conflict32571D → Y in CAA58836. Ref.1
Sequence conflict32571D → Y in CAA58837. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified October 16, 2013. Version 4.
Checksum: 993EB20BACDD6C59

FASTA3,330366,227
        10         20         30         40         50         60 
MAVALGRAPR SLPLLLTLLL LLLLRMSPSW SVVGQDHPMS SRSLHPPYFN LAQAARIWAT 

        70         80         90        100        110        120 
ATCGERDPEV SRPRPELFCK LVGGPAAQGS GHTIQGQFCD YCNSEDSRKA HPASHAIDGS 

       130        140        150        160        170        180 
ERWWQSPPLS SGTQYNQVNL TLDLGQLFHV AYILIKFANS PRPDLWILER SVDFGSTYSP 

       190        200        210        220        230        240 
WQYFAHSRRD CVEQFGQEAN MAITQDDQML CVTEYSRIVP LENGEIVVSL INGRPGAKKF 

       250        260        270        280        290        300 
AFSDTLREFT KATNIRLRFL RTNTLLGHLI SKAERDPTVT RRYYYSIKDI SVGGRCVCNG 

       310        320        330        340        350        360 
HAEACSADNP EKQFRCECQH HTCGDTCNRC CAGYNQRRWQ PAGQEQHNEC EACNCHGHAV 

       370        380        390        400        410        420 
DCYYDPDVEH QQASLNSKGV YAGGGVCINC QHNTAGVNCE KCAKGYFRPH GVPVDALHGC 

       430        440        450        460        470        480 
IPCSCDPERA DDCDQGSGHC HCKPNFSGDY CETCADGYYN FPFCLRIPVF PNYTPSPEDP 

       490        500        510        520        530        540 
VAGNIKGCDC NLEGVLPEIC DDRGRCLCRP GVEGPQCDSC RSGSYSFPIC QACQCSTIGS 

       550        560        570        580        590        600 
YPVPCDPGNG QCDCLPGITG RQCDRCLSGA YDFPYCQGSG SVCHPAGTLD SSLGYCQCKQ 

       610        620        630        640        650        660 
HVASPTCSVC KPLYWNLAKE NPRGCSECQC HEAGTLSGIG ECGQEDGDCS CKAHVTGDAC 

       670        680        690        700        710        720 
DTCEDGFFSL EKSNYFGCQG CQCDIGGALT TMCSGPSGVC QCREHVEGKQ CQRPENNYYF 

       730        740        750        760        770        780 
PDLHHMKYEV EDGTGPNGRN LRFGFDPLVF PEFSWRGYAP MTSVQNEVRV RLSVRQSSLS 

       790        800        810        820        830        840 
LFRIVLRYIS PGTEAISGRI TLYSSQGDSD ALQSRKITFP PSKEPAFVTV PGNGFAGPFS 

       850        860        870        880        890        900 
ITPGTWIACI QVEGVLLDYL VLLPRDYYEA FTLQVPVTEP CAHTGSPQDN CLLYQHLPLT 

       910        920        930        940        950        960 
AFSCTLACEA RHFLLDGELR PLAMRQPTPT HPAMVDLSGR EVELQLRLRV PQVGHYVVLL 

       970        980        990       1000       1010       1020 
EYATEVEQLF VVDVNLKSSG SALAGQVNIY SCKYSIPCRS VVIDSLSRTA VHELLADADI 

      1030       1040       1050       1060       1070       1080 
QLKAHMAHFL LYHICIIPAE EFSTEYLRPQ VHCIASYRQH ANPSASCVSL AHETPPTASI 

      1090       1100       1110       1120       1130       1140 
LDATSRGLFS ALPHEPSSPA DGVTLKAPQS QVTLKGLIPH LGRHVFVIHF YQAEHPGFPT 

      1150       1160       1170       1180       1190       1200 
EVIVNGGRQW SGSFLASFCP HLLGCRDQVI SDGQVEFDIS EAEVAVTVKI PDGKSLTLVR 

      1210       1220       1230       1240       1250       1260 
VLVVPAENYD YQILHKTTVD KSSEFISSCG GDSFYIDPQA ASGFCKNSAR SLVAFYHNGA 

      1270       1280       1290       1300       1310       1320 
IPCECDPAGT AGHHCSPEGG QCPCRPNVIG RQCSRCATGY YGFPYCKPCN CGRRLCEEVT 

      1330       1340       1350       1360       1370       1380 
GKCLCPPHTV RPQCEVCEMN SFNFHPVAGC DVCNCSRKGT IEAAVSECDR DSGQCRCKPR 

      1390       1400       1410       1420       1430       1440 
VTGQQCDKCA PGFYQFPECV PCSCNRDGTE PSVCDPETGA CMCKENVEGP QCQLCREGSF 

      1450       1460       1470       1480       1490       1500 
YLDPTNPKGC TKCFCFGVNT DCQSSHKQRA KFVDMMGWRL ETADGVDVPV SFNPGSNSMV 

      1510       1520       1530       1540       1550       1560 
ADLQELPPSV HSASWVAPPS YLGDKVSSYG GYLTYHAKSF GLPGDMVLLG KQPDVQLTGQ 

      1570       1580       1590       1600       1610       1620 
HMSLIHKEPS DPRPDRLHHG RVQVIEGNFR HEGSSAPVSR EELMTVLSRL ERLHIRGLHF 

      1630       1640       1650       1660       1670       1680 
TETQRLTLGE VGLEEASDTG SGPRAHLVEM CACPPDYTGD SCQGCRPGYY WDNKSLPVGR 

      1690       1700       1710       1720       1730       1740 
CVPCNCNGHS NRCQDGSGIC INCQHNTAGE HCERCQAGHY GNAIHGSCRV CPCPHTNSFA 

      1750       1760       1770       1780       1790       1800 
TGCAVDGGAV RCACKPGYTG TQCERCAPGY FGNPQKFGGS CQPCNCNSNG QLGPCDPLTG 

      1810       1820       1830       1840       1850       1860 
DCVNQEPKDG SPAEECDDCD SCVMTLLNDL ASMGEELRLV KSKLQGLSVS TGALEQIRHM 

      1870       1880       1890       1900       1910       1920 
ETQAKDLRNQ LLGFRSATSS HGSKMDDLEK ELSHLNREFE TLQEKAQVNS RKAQTLYNNI 

      1930       1940       1950       1960       1970       1980 
DQTIQSAKEL DMKIKNIVQN VHILLKQMAR PGGEGTDLPV GDWSRELAEA QRMMRDLRSR 

      1990       2000       2010       2020       2030       2040 
DFKKHLQEAE AEKMEAQLLL HRIRTWLESH QVENNGLLKN IRDSLNDYED KLQDLRSILQ 

      2050       2060       2070       2080       2090       2100 
EAAAQAKQAT GINHENEGVL GAIQRQMKEM DSLKNDFTKY LATADSSLLQ TNNLLQQMDK 

      2110       2120       2130       2140       2150       2160 
SQKEYESLAA ALNGARQELS DRVRELSRSG GKAPLVVEAE KHAQSLQELA KQLEEIKRNT 

      2170       2180       2190       2200       2210       2220 
SGDELVRCAV DAATAYENIL NAIRAAEDAA SKATSASKSA FQTVIKEDLP KRAKTLSSDS 

      2230       2240       2250       2260       2270       2280 
EELLNEAKMT QKRLQQVSPA LNSLQQTLKT VSVQKDLLDA NLTVARDDLH GIQRGDIDSV 

      2290       2300       2310       2320       2330       2340 
VIGAKSMVRE ANGITSEVLD GLNPIQTDLG RIKDSYESAR REDFSKALVD ANNSVKKLTR 

      2350       2360       2370       2380       2390       2400 
KLPDLFIKIE SINQQLLPLG NISDNVDRIR ELIQQARDAA NKVAIPMRFN GKSGVEVRLP 

      2410       2420       2430       2440       2450       2460 
NDLEDLKGYT SLSLFLQRPD LRENGGTEDM FVMYLGNKDA SKDYIGMAVV DGQLTCVYNL 

      2470       2480       2490       2500       2510       2520 
GDREAEVQID QVLTESESQE AVMDRVKFQR IYQFAKLNYT KEATSTKPKA PGVYDMESAS 

      2530       2540       2550       2560       2570       2580 
SNTLLNLDPE NAVFYVGGYP PGFELPRRLR FPPYKGCIEL DDLNENVLSL YNFKTTFNLN 

      2590       2600       2610       2620       2630       2640 
TTEVEPCRRR KEESDKNYFE GTGYARIPTQ PNAPFPNFMQ TIQTTVDRGL LFFAENQDNF 

      2650       2660       2670       2680       2690       2700 
ISLNIEDGNL MVKYKLNSEP PKEKGIRDTI NNGRDHMILI SIGKSQKRML INMNKHSIII 

      2710       2720       2730       2740       2750       2760 
EGEIFDFSTY YLGGIPIAIR ERFNISTPAF QGCMKNLKKT SGVVRLNDTV GVTKKCSEDW 

      2770       2780       2790       2800       2810       2820 
KLVRTASFSR GGQMSFTNLD VPSLDRFQLS FGFQTFQPSG TLLNHQTRTS SLLVTLEDGH 

      2830       2840       2850       2860       2870       2880 
IALSTRDSSS PIFKSPGTYM DGLLHHVSVI SDTSGLRLLI DDQVLRRNQR LASFSNAQQS 

      2890       2900       2910       2920       2930       2940 
LSMGGGYFEG CISNVFVQRM SQSPEVLDMA SKSTKRDAFL GGCSLNKPPF LMLFKSPKGF 

      2950       2960       2970       2980       2990       3000 
NKARSFNVNQ LLQDAPQAAR SIEAWQDGKS CLPPLNTKAT HRALQFGDSP TSHLLFKLPQ 

      3010       3020       3030       3040       3050       3060 
ELLKPRLQFS LDIQTTSSRG LVFHTGTRDS FVALYLSEGH VIFALGAGGK KLRLRSKERY 

      3070       3080       3090       3100       3110       3120 
HDGKWHSVVF GLSGRKVHLV VDGLRAQEGS LPGNSTISPR EQVYLGLSPS RKSKSLPQHS 

      3130       3140       3150       3160       3170       3180 
FVGCLRNFQL DSKPLDSPSA RSGVSPCLGG SLEKGIYFSQ GGGHVVLANS VSLEPALTLT 

      3190       3200       3210       3220       3230       3240 
LSIRPRSLTG VLIHIASQSG EHLSVYMEAG KVTTSMNSEA GGTVTSITPK RSLCDGQWHS 

      3250       3260       3270       3280       3290       3300 
VTVSIKQHTL HLELDTDNSY TAGQLSFPPN STRGSLHIGG VPDKLKMLTL PVWNSFFGCL 

      3310       3320       3330 
KNIQVNHIPV PITEATDVQG SVSLNGCPDH 

« Hide

Isoform A [UniParc].

Checksum: 01153704F6DC87C3
Show »

FASTA1,724190,610

References

« Hide 'large scale' references
[1]"Cloning and complete primary structure of the mouse laminin alpha 3 chain. Distinct expression pattern of the laminin alpha 3A and alpha 3B chain isoforms."
Galliano M.-F., Aberdam D., Aguzzi A., Ortonne J.-P., Meneguzzi G.
J. Biol. Chem. 270:21820-21826(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [MRNA] OF 765-3330 (ISOFORM B).
Strain: BALB/c.
Tissue: Lung.
[2]Aberdam D.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Complete sequence, recombinant analysis and binding to laminins and sulphated ligands of the N-terminal domains of laminin alpha3B and alpha5 chains."
Garbe J.H., Gohring W., Mann K., Timpl R., Sasaki T.
Biochem. J. 362:213-221(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-58 (ISOFORM B), PROTEIN SEQUENCE OF 32-38.
[5]"The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform."
Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D., Jenkins N.A., Copeland N.G., Sanes J.R.
J. Cell Biol. 137:685-701(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-776 (ISOFORM B).
Strain: ICR.
[6]"Assignment of mouse nicein genes to chromosomes 1 and 18."
Aberdam D., Galliano M.-F., Mattei M.-G., Pisani-Spadafora A., Ortonne J.-P., Meneguzzi G.
Mamm. Genome 5:229-233(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1813-2531 (ISOFORM B).
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84013 mRNA. Translation: CAA58836.1.
X84014 mRNA. Translation: CAA58837.1. Frameshift.
AC102131 Genomic DNA. No translation available.
AC102248 Genomic DNA. No translation available.
AC139027 Genomic DNA. No translation available.
AC157909 Genomic DNA. No translation available.
AJ293592 mRNA. Translation: CAB99254.2.
U88353 mRNA. Translation: AAC53179.1.
L20478 mRNA. Translation: AAA68091.1.
RefSeqNP_034810.1. NM_010680.1.
XP_006525753.1. XM_006525690.1.
UniGeneMm.42012.

3D structure databases

ProteinModelPortalQ61789.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ61789.

Proteomic databases

PaxDbQ61789.
PRIDEQ61789.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092070; ENSMUSP00000089703; ENSMUSG00000024421. [Q61789-1]
GeneID16774.
KEGGmmu:16774.

Organism-specific databases

CTD3909.
MGIMGI:99909. Lama3.

Phylogenomic databases

eggNOGNOG292643.
GeneTreeENSGT00750000117549.
HOGENOMHOG000048708.
HOVERGENHBG052300.
KOK06240.
OrthoDBEOG7DFXB9.
TreeFamTF335359.

Gene expression databases

BgeeE9PUR4.
CleanExMM_LAMA3.
GenevestigatorQ61789.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 13 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 4 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 13 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 5 hits.
PROSITEPS00022. EGF_1. 11 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 12 hits.
PS50027. EGF_LAM_2. 13 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
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NextBio290610.
PROQ61789.
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Entry information

Entry nameLAMA3_MOUSE
AccessionPrimary (citable) accession number: Q61789
Secondary accession number(s): E9PUR4 expand/collapse secondary AC list , O08751, Q61788, Q61966, Q9JHQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 16, 2013
Last modified: April 16, 2014
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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