Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q61789

- LAMA3_MOUSE

UniProt

Q61789 - LAMA3_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Laminin subunit alpha-3

Gene

Lama3

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.
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

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. regulation of cell adhesion Source: InterPro
  3. regulation of cell migration Source: InterPro
  4. regulation of embryonic development Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_262098. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Lama3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:99909. Lama3.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. extracellular region Source: Reactome
  3. laminin-1 complex Source: InterPro
  4. 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 – 31311 PublicationAdd
BLAST
Chaini32 – 33303299Laminin subunit alpha-3PRO_0000017059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi296 ↔ 305By similarity
Disulfide bondi298 ↔ 316By similarity
Disulfide bondi318 ↔ 327By similarity
Disulfide bondi330 ↔ 350By similarity
Disulfide bondi353 ↔ 362By similarity
Disulfide bondi355 ↔ 387By similarity
Disulfide bondi390 ↔ 399By similarity
Disulfide bondi402 ↔ 420By similarity
Disulfide bondi423 ↔ 433By similarity
Disulfide bondi425 ↔ 440By similarity
Disulfide bondi442 ↔ 451By similarity
Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi454 ↔ 464By similarity
Disulfide bondi488 ↔ 500By similarity
Disulfide bondi490 ↔ 506By similarity
Disulfide bondi508 ↔ 517By similarity
Disulfide bondi520 ↔ 530By similarity
Disulfide bondi533 ↔ 545By similarity
Disulfide bondi535 ↔ 552By similarity
Disulfide bondi554 ↔ 563By similarity
Disulfide bondi566 ↔ 583By similarity
Disulfide bondi628 ↔ 642By similarity
Disulfide bondi630 ↔ 649By similarity
Disulfide bondi651 ↔ 660By similarity
Disulfide bondi663 ↔ 678By similarity
Disulfide bondi681 ↔ 693By similarity
Disulfide bondi683 ↔ 700By similarity
Disulfide bondi702 ↔ 711By similarity
Disulfide bondi1309 ↔ 1316By similarity
Disulfide bondi1311 ↔ 1323By similarity
Disulfide bondi1325 ↔ 1334By similarity
Disulfide bondi1337 ↔ 1350By similarity
Disulfide bondi1353 ↔ 1368By similarity
Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1355 ↔ 1375By similarity
Disulfide bondi1377 ↔ 1386By similarity
Disulfide bondi1389 ↔ 1399By similarity
Disulfide bondi1402 ↔ 1414By similarity
Disulfide bondi1404 ↔ 1421By similarity
Disulfide bondi1423 ↔ 1432By similarity
Disulfide bondi1435 ↔ 1450By similarity
Glycosylationi1673 – 16731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1684 ↔ 1693By similarity
Disulfide bondi1686 ↔ 1700By similarity
Disulfide bondi1703 ↔ 1712By similarity
Disulfide bondi1715 ↔ 1728By similarity
Disulfide bondi1731 ↔ 1743By similarity
Disulfide bondi1733 ↔ 1752By similarity
Disulfide bondi1754 ↔ 1763By similarity
Disulfide bondi1766 ↔ 1781By similarity
Disulfide bondi1819 – 1819InterchainCurated
Disulfide bondi1822 – 1822InterchainCurated
Glycosylationi2159 – 21591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2261 – 22611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2332 – 23321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2361 – 23611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2498 – 24981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2557 ↔ 2587By similarity
Glycosylationi2580 – 25801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2733 ↔ 2756By similarity
Glycosylationi2747 – 27471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2891 ↔ 2923By similarity
Glycosylationi3094 – 30941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3124 ↔ 3147By similarity
Glycosylationi3270 – 32701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3299 ↔ 3327By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61789.
PaxDbiQ61789.
PRIDEiQ61789.

PTM databases

PhosphoSiteiQ61789.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiE9PUR4.
CleanExiMM_LAMA3.
GenevestigatoriQ61789.

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. 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).

Structurei

3D structure databases

ProteinModelPortaliQ61789.
SMRiQ61789. Positions 43-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 295256Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini296 – 35055Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini353 – 42068Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 46442Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini488 – 53043Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini533 – 57644Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini582 – 62544Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini628 – 67851Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini681 – 72545Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini1309 – 135244Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini1353 – 140149Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1402 – 145251Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1453 – 146210Laminin EGF-like 12; first partPROSITE-ProRule annotation
Domaini1466 – 1650185Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini1651 – 168333Laminin EGF-like 12; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1684 – 173047Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1731 – 178353Laminin EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini1784 – 181835Laminin EGF-like 15; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini2386 – 2587202Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2594 – 2756163Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini2763 – 2923161Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini2983 – 3147165Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini3154 – 3327174Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni295 – 725431Domain VAdd
BLAST
Regioni793 – 1262470Domain IV 1 (domain IV B)Add
BLAST
Regioni1263 – 1462200Domain III BAdd
BLAST
Regioni1651 – 1818168Domain III AAdd
BLAST
Regioni1819 – 2385567Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1851 – 1980130Sequence AnalysisAdd
BLAST
Coiled coili2012 – 205746Sequence AnalysisAdd
BLAST
Coiled coili2088 – 216578Sequence AnalysisAdd
BLAST
Coiled coili2211 – 223828Sequence AnalysisAdd
BLAST
Coiled coili2318 – 238366Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2274 – 22763Cell attachment siteSequence Analysis

Domaini

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 similaritiesi

Contains 15 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-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

eggNOGiNOG292643.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000048708.
HOVERGENiHBG052300.
InParanoidiQ61789.
KOiK06240.
OMAiRGLYFTE.
OrthoDBiEOG7DFXB9.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. 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]
SMARTiSM00180. EGF_Lam. 13 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform B (identifier: Q61789-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAVALGRAPR SLPLLLTLLL LLLLRMSPSW SVVGQDHPMS SRSLHPPYFN
60 70 80 90 100
LAQAARIWAT ATCGERDPEV SRPRPELFCK LVGGPAAQGS GHTIQGQFCD
110 120 130 140 150
YCNSEDSRKA HPASHAIDGS ERWWQSPPLS SGTQYNQVNL TLDLGQLFHV
160 170 180 190 200
AYILIKFANS PRPDLWILER SVDFGSTYSP WQYFAHSRRD CVEQFGQEAN
210 220 230 240 250
MAITQDDQML CVTEYSRIVP LENGEIVVSL INGRPGAKKF AFSDTLREFT
260 270 280 290 300
KATNIRLRFL RTNTLLGHLI SKAERDPTVT RRYYYSIKDI SVGGRCVCNG
310 320 330 340 350
HAEACSADNP EKQFRCECQH HTCGDTCNRC CAGYNQRRWQ PAGQEQHNEC
360 370 380 390 400
EACNCHGHAV DCYYDPDVEH QQASLNSKGV YAGGGVCINC QHNTAGVNCE
410 420 430 440 450
KCAKGYFRPH GVPVDALHGC IPCSCDPERA DDCDQGSGHC HCKPNFSGDY
460 470 480 490 500
CETCADGYYN FPFCLRIPVF PNYTPSPEDP VAGNIKGCDC NLEGVLPEIC
510 520 530 540 550
DDRGRCLCRP GVEGPQCDSC RSGSYSFPIC QACQCSTIGS YPVPCDPGNG
560 570 580 590 600
QCDCLPGITG RQCDRCLSGA YDFPYCQGSG SVCHPAGTLD SSLGYCQCKQ
610 620 630 640 650
HVASPTCSVC KPLYWNLAKE NPRGCSECQC HEAGTLSGIG ECGQEDGDCS
660 670 680 690 700
CKAHVTGDAC DTCEDGFFSL EKSNYFGCQG CQCDIGGALT TMCSGPSGVC
710 720 730 740 750
QCREHVEGKQ CQRPENNYYF PDLHHMKYEV EDGTGPNGRN LRFGFDPLVF
760 770 780 790 800
PEFSWRGYAP MTSVQNEVRV RLSVRQSSLS LFRIVLRYIS PGTEAISGRI
810 820 830 840 850
TLYSSQGDSD ALQSRKITFP PSKEPAFVTV PGNGFAGPFS ITPGTWIACI
860 870 880 890 900
QVEGVLLDYL VLLPRDYYEA FTLQVPVTEP CAHTGSPQDN CLLYQHLPLT
910 920 930 940 950
AFSCTLACEA RHFLLDGELR PLAMRQPTPT HPAMVDLSGR EVELQLRLRV
960 970 980 990 1000
PQVGHYVVLL EYATEVEQLF VVDVNLKSSG SALAGQVNIY SCKYSIPCRS
1010 1020 1030 1040 1050
VVIDSLSRTA VHELLADADI QLKAHMAHFL LYHICIIPAE EFSTEYLRPQ
1060 1070 1080 1090 1100
VHCIASYRQH ANPSASCVSL AHETPPTASI LDATSRGLFS ALPHEPSSPA
1110 1120 1130 1140 1150
DGVTLKAPQS QVTLKGLIPH LGRHVFVIHF YQAEHPGFPT EVIVNGGRQW
1160 1170 1180 1190 1200
SGSFLASFCP HLLGCRDQVI SDGQVEFDIS EAEVAVTVKI PDGKSLTLVR
1210 1220 1230 1240 1250
VLVVPAENYD YQILHKTTVD KSSEFISSCG GDSFYIDPQA ASGFCKNSAR
1260 1270 1280 1290 1300
SLVAFYHNGA IPCECDPAGT AGHHCSPEGG QCPCRPNVIG RQCSRCATGY
1310 1320 1330 1340 1350
YGFPYCKPCN CGRRLCEEVT GKCLCPPHTV RPQCEVCEMN SFNFHPVAGC
1360 1370 1380 1390 1400
DVCNCSRKGT IEAAVSECDR DSGQCRCKPR VTGQQCDKCA PGFYQFPECV
1410 1420 1430 1440 1450
PCSCNRDGTE PSVCDPETGA CMCKENVEGP QCQLCREGSF YLDPTNPKGC
1460 1470 1480 1490 1500
TKCFCFGVNT DCQSSHKQRA KFVDMMGWRL ETADGVDVPV SFNPGSNSMV
1510 1520 1530 1540 1550
ADLQELPPSV HSASWVAPPS YLGDKVSSYG GYLTYHAKSF GLPGDMVLLG
1560 1570 1580 1590 1600
KQPDVQLTGQ HMSLIHKEPS DPRPDRLHHG RVQVIEGNFR HEGSSAPVSR
1610 1620 1630 1640 1650
EELMTVLSRL ERLHIRGLHF TETQRLTLGE VGLEEASDTG SGPRAHLVEM
1660 1670 1680 1690 1700
CACPPDYTGD SCQGCRPGYY WDNKSLPVGR CVPCNCNGHS NRCQDGSGIC
1710 1720 1730 1740 1750
INCQHNTAGE HCERCQAGHY GNAIHGSCRV CPCPHTNSFA TGCAVDGGAV
1760 1770 1780 1790 1800
RCACKPGYTG TQCERCAPGY FGNPQKFGGS CQPCNCNSNG QLGPCDPLTG
1810 1820 1830 1840 1850
DCVNQEPKDG SPAEECDDCD SCVMTLLNDL ASMGEELRLV KSKLQGLSVS
1860 1870 1880 1890 1900
TGALEQIRHM ETQAKDLRNQ LLGFRSATSS HGSKMDDLEK ELSHLNREFE
1910 1920 1930 1940 1950
TLQEKAQVNS RKAQTLYNNI DQTIQSAKEL DMKIKNIVQN VHILLKQMAR
1960 1970 1980 1990 2000
PGGEGTDLPV GDWSRELAEA QRMMRDLRSR DFKKHLQEAE AEKMEAQLLL
2010 2020 2030 2040 2050
HRIRTWLESH QVENNGLLKN IRDSLNDYED KLQDLRSILQ EAAAQAKQAT
2060 2070 2080 2090 2100
GINHENEGVL GAIQRQMKEM DSLKNDFTKY LATADSSLLQ TNNLLQQMDK
2110 2120 2130 2140 2150
SQKEYESLAA ALNGARQELS DRVRELSRSG GKAPLVVEAE KHAQSLQELA
2160 2170 2180 2190 2200
KQLEEIKRNT SGDELVRCAV DAATAYENIL NAIRAAEDAA SKATSASKSA
2210 2220 2230 2240 2250
FQTVIKEDLP KRAKTLSSDS EELLNEAKMT QKRLQQVSPA LNSLQQTLKT
2260 2270 2280 2290 2300
VSVQKDLLDA NLTVARDDLH GIQRGDIDSV VIGAKSMVRE ANGITSEVLD
2310 2320 2330 2340 2350
GLNPIQTDLG RIKDSYESAR REDFSKALVD ANNSVKKLTR KLPDLFIKIE
2360 2370 2380 2390 2400
SINQQLLPLG NISDNVDRIR ELIQQARDAA NKVAIPMRFN GKSGVEVRLP
2410 2420 2430 2440 2450
NDLEDLKGYT SLSLFLQRPD LRENGGTEDM FVMYLGNKDA SKDYIGMAVV
2460 2470 2480 2490 2500
DGQLTCVYNL GDREAEVQID QVLTESESQE AVMDRVKFQR IYQFAKLNYT
2510 2520 2530 2540 2550
KEATSTKPKA PGVYDMESAS SNTLLNLDPE NAVFYVGGYP PGFELPRRLR
2560 2570 2580 2590 2600
FPPYKGCIEL DDLNENVLSL YNFKTTFNLN TTEVEPCRRR KEESDKNYFE
2610 2620 2630 2640 2650
GTGYARIPTQ PNAPFPNFMQ TIQTTVDRGL LFFAENQDNF ISLNIEDGNL
2660 2670 2680 2690 2700
MVKYKLNSEP PKEKGIRDTI NNGRDHMILI SIGKSQKRML INMNKHSIII
2710 2720 2730 2740 2750
EGEIFDFSTY YLGGIPIAIR ERFNISTPAF QGCMKNLKKT SGVVRLNDTV
2760 2770 2780 2790 2800
GVTKKCSEDW KLVRTASFSR GGQMSFTNLD VPSLDRFQLS FGFQTFQPSG
2810 2820 2830 2840 2850
TLLNHQTRTS SLLVTLEDGH IALSTRDSSS PIFKSPGTYM DGLLHHVSVI
2860 2870 2880 2890 2900
SDTSGLRLLI DDQVLRRNQR LASFSNAQQS LSMGGGYFEG CISNVFVQRM
2910 2920 2930 2940 2950
SQSPEVLDMA SKSTKRDAFL GGCSLNKPPF LMLFKSPKGF NKARSFNVNQ
2960 2970 2980 2990 3000
LLQDAPQAAR SIEAWQDGKS CLPPLNTKAT HRALQFGDSP TSHLLFKLPQ
3010 3020 3030 3040 3050
ELLKPRLQFS LDIQTTSSRG LVFHTGTRDS FVALYLSEGH VIFALGAGGK
3060 3070 3080 3090 3100
KLRLRSKERY HDGKWHSVVF GLSGRKVHLV VDGLRAQEGS LPGNSTISPR
3110 3120 3130 3140 3150
EQVYLGLSPS RKSKSLPQHS FVGCLRNFQL DSKPLDSPSA RSGVSPCLGG
3160 3170 3180 3190 3200
SLEKGIYFSQ GGGHVVLANS VSLEPALTLT LSIRPRSLTG VLIHIASQSG
3210 3220 3230 3240 3250
EHLSVYMEAG KVTTSMNSEA GGTVTSITPK RSLCDGQWHS VTVSIKQHTL
3260 3270 3280 3290 3300
HLELDTDNSY TAGQLSFPPN STRGSLHIGG VPDKLKMLTL PVWNSFFGCL
3310 3320 3330
KNIQVNHIPV PITEATDVQG SVSLNGCPDH
Length:3,330
Mass (Da):366,227
Last modified:October 16, 2013 - v4
Checksum:i993EB20BACDD6C59
GO
Isoform A (identifier: Q61789-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,724
Mass (Da):190,610
Checksum:i01153704F6DC87C3
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti982 – 9821A → R in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1150 – 11501W → R in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1224 – 12241E → K in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1272 – 12721G → GH in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1291 – 12911R → S in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1398 – 13981E → K in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1466 – 14661H → R in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1479 – 14791R → V in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1488 – 14881V → F in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1527 – 15282SS → II in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1608 – 16081S → P in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1983 – 19842KK → QN in CAA58836. (PubMed:7665604)Curated
Sequence conflicti1983 – 19842KK → QN in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1983 – 19842KK → QN in AAA68091. (PubMed:8012114)Curated
Sequence conflicti1987 – 19871Q → G in CAA58836. (PubMed:7665604)Curated
Sequence conflicti1987 – 19871Q → G in CAA58837. (PubMed:7665604)Curated
Sequence conflicti1987 – 19871Q → G in AAA68091. (PubMed:8012114)Curated
Sequence conflicti2463 – 24631R → G in CAA58836. (PubMed:7665604)Curated
Sequence conflicti2463 – 24631R → G in CAA58837. (PubMed:7665604)Curated
Sequence conflicti2463 – 24631R → G in AAA68091. (PubMed:8012114)Curated
Sequence conflicti2488 – 24881F → S in CAA58836. (PubMed:7665604)Curated
Sequence conflicti2488 – 24881F → S in CAA58837. (PubMed:7665604)Curated
Sequence conflicti2488 – 24881F → S in AAA68091. (PubMed:8012114)Curated
Sequence conflicti2617 – 26204NFMQ → KLSW in CAA58836. (PubMed:7665604)Curated
Sequence conflicti2617 – 26204NFMQ → KLSW in CAA58837. (PubMed:7665604)Curated
Sequence conflicti2724 – 27252NI → PL in CAA58836. (PubMed:7665604)Curated
Sequence conflicti2724 – 27252NI → PL in CAA58837. (PubMed:7665604)Curated
Sequence conflicti3257 – 32571D → Y in CAA58836. (PubMed:7665604)Curated
Sequence conflicti3257 – 32571D → Y in CAA58837. (PubMed:7665604)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 16191619Missing in isoform A. 1 PublicationVSP_003038Add
BLAST
Alternative sequencei1620 – 166243FTETQ…TGDSC → MLPAVRWSAWSTGWLWIFGA ALGQCLGYGSEQQRVAFLQR PSQNHLQASYMELRPS in isoform A. 1 PublicationVSP_003039Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS50222.1. [Q61789-1]
RefSeqiNP_034810.1. NM_010680.1. [Q61789-1]
XP_006525753.1. XM_006525690.1. [Q61789-2]
UniGeneiMm.42012.

Genome annotation databases

EnsembliENSMUST00000092070; ENSMUSP00000089703; ENSMUSG00000024421. [Q61789-1]
ENSMUST00000188815; ENSMUSP00000140104; ENSMUSG00000024421. [Q61789-2]
GeneIDi16774.
KEGGimmu:16774.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS50222.1. [Q61789-1 ]
RefSeqi NP_034810.1. NM_010680.1. [Q61789-1 ]
XP_006525753.1. XM_006525690.1. [Q61789-2 ]
UniGenei Mm.42012.

3D structure databases

ProteinModelPortali Q61789.
SMRi Q61789. Positions 43-424.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q61789.

Proteomic databases

MaxQBi Q61789.
PaxDbi Q61789.
PRIDEi Q61789.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000092070 ; ENSMUSP00000089703 ; ENSMUSG00000024421 . [Q61789-1 ]
ENSMUST00000188815 ; ENSMUSP00000140104 ; ENSMUSG00000024421 . [Q61789-2 ]
GeneIDi 16774.
KEGGi mmu:16774.

Organism-specific databases

CTDi 3909.
MGIi MGI:99909. Lama3.

Phylogenomic databases

eggNOGi NOG292643.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000048708.
HOVERGENi HBG052300.
InParanoidi Q61789.
KOi K06240.
OMAi RGLYFTE.
OrthoDBi EOG7DFXB9.
TreeFami TF335359.

Enzyme and pathway databases

Reactomei REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_262098. Type I hemidesmosome assembly.

Miscellaneous databases

NextBioi 290610.
PROi Q61789.
SOURCEi Search...

Gene expression databases

Bgeei E9PUR4.
CleanExi MM_LAMA3.
Genevestigatori Q61789.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. 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 ]
SMARTi SM00180. EGF_Lam. 13 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 5 hits.
PROSITEi PS00022. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1813-2531 (ISOFORM B).
    Tissue: Lung.

Entry informationi

Entry nameiLAMA3_MOUSE
AccessioniPrimary (citable) accession number: Q61789
Secondary accession number(s): E9PUR4
, O08751, Q61788, Q61966, Q9JHQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 16, 2013
Last modified: November 26, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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