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Q61789

- LAMA3_MOUSE

UniProt

Q61789 - LAMA3_MOUSE

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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_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

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 Publication
Add
BLAST
Chaini32 – 33303299Laminin subunit alpha-3
PRO_0000017059Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2274 – 22763Cell attachment site Reviewed prediction

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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG292643.
GeneTreeiENSGT00750000117549.
HOGENOMiHOG000048708.
HOVERGENiHBG052300.
KOiK06240.
OMAiRGLYFTE.
OrthoDBiEOG7DFXB9.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR008985. 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]
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

MAVALGRAPR SLPLLLTLLL LLLLRMSPSW SVVGQDHPMS SRSLHPPYFN     50
LAQAARIWAT ATCGERDPEV SRPRPELFCK LVGGPAAQGS GHTIQGQFCD 100
YCNSEDSRKA HPASHAIDGS ERWWQSPPLS SGTQYNQVNL TLDLGQLFHV 150
AYILIKFANS PRPDLWILER SVDFGSTYSP WQYFAHSRRD CVEQFGQEAN 200
MAITQDDQML CVTEYSRIVP LENGEIVVSL INGRPGAKKF AFSDTLREFT 250
KATNIRLRFL RTNTLLGHLI SKAERDPTVT RRYYYSIKDI SVGGRCVCNG 300
HAEACSADNP EKQFRCECQH HTCGDTCNRC CAGYNQRRWQ PAGQEQHNEC 350
EACNCHGHAV DCYYDPDVEH QQASLNSKGV YAGGGVCINC QHNTAGVNCE 400
KCAKGYFRPH GVPVDALHGC IPCSCDPERA DDCDQGSGHC HCKPNFSGDY 450
CETCADGYYN FPFCLRIPVF PNYTPSPEDP VAGNIKGCDC NLEGVLPEIC 500
DDRGRCLCRP GVEGPQCDSC RSGSYSFPIC QACQCSTIGS YPVPCDPGNG 550
QCDCLPGITG RQCDRCLSGA YDFPYCQGSG SVCHPAGTLD SSLGYCQCKQ 600
HVASPTCSVC KPLYWNLAKE NPRGCSECQC HEAGTLSGIG ECGQEDGDCS 650
CKAHVTGDAC DTCEDGFFSL EKSNYFGCQG CQCDIGGALT TMCSGPSGVC 700
QCREHVEGKQ CQRPENNYYF PDLHHMKYEV EDGTGPNGRN LRFGFDPLVF 750
PEFSWRGYAP MTSVQNEVRV RLSVRQSSLS LFRIVLRYIS PGTEAISGRI 800
TLYSSQGDSD ALQSRKITFP PSKEPAFVTV PGNGFAGPFS ITPGTWIACI 850
QVEGVLLDYL VLLPRDYYEA FTLQVPVTEP CAHTGSPQDN CLLYQHLPLT 900
AFSCTLACEA RHFLLDGELR PLAMRQPTPT HPAMVDLSGR EVELQLRLRV 950
PQVGHYVVLL EYATEVEQLF VVDVNLKSSG SALAGQVNIY SCKYSIPCRS 1000
VVIDSLSRTA VHELLADADI QLKAHMAHFL LYHICIIPAE EFSTEYLRPQ 1050
VHCIASYRQH ANPSASCVSL AHETPPTASI LDATSRGLFS ALPHEPSSPA 1100
DGVTLKAPQS QVTLKGLIPH LGRHVFVIHF YQAEHPGFPT EVIVNGGRQW 1150
SGSFLASFCP HLLGCRDQVI SDGQVEFDIS EAEVAVTVKI PDGKSLTLVR 1200
VLVVPAENYD YQILHKTTVD KSSEFISSCG GDSFYIDPQA ASGFCKNSAR 1250
SLVAFYHNGA IPCECDPAGT AGHHCSPEGG QCPCRPNVIG RQCSRCATGY 1300
YGFPYCKPCN CGRRLCEEVT GKCLCPPHTV RPQCEVCEMN SFNFHPVAGC 1350
DVCNCSRKGT IEAAVSECDR DSGQCRCKPR VTGQQCDKCA PGFYQFPECV 1400
PCSCNRDGTE PSVCDPETGA CMCKENVEGP QCQLCREGSF YLDPTNPKGC 1450
TKCFCFGVNT DCQSSHKQRA KFVDMMGWRL ETADGVDVPV SFNPGSNSMV 1500
ADLQELPPSV HSASWVAPPS YLGDKVSSYG GYLTYHAKSF GLPGDMVLLG 1550
KQPDVQLTGQ HMSLIHKEPS DPRPDRLHHG RVQVIEGNFR HEGSSAPVSR 1600
EELMTVLSRL ERLHIRGLHF TETQRLTLGE VGLEEASDTG SGPRAHLVEM 1650
CACPPDYTGD SCQGCRPGYY WDNKSLPVGR CVPCNCNGHS NRCQDGSGIC 1700
INCQHNTAGE HCERCQAGHY GNAIHGSCRV CPCPHTNSFA TGCAVDGGAV 1750
RCACKPGYTG TQCERCAPGY FGNPQKFGGS CQPCNCNSNG QLGPCDPLTG 1800
DCVNQEPKDG SPAEECDDCD SCVMTLLNDL ASMGEELRLV KSKLQGLSVS 1850
TGALEQIRHM ETQAKDLRNQ LLGFRSATSS HGSKMDDLEK ELSHLNREFE 1900
TLQEKAQVNS RKAQTLYNNI DQTIQSAKEL DMKIKNIVQN VHILLKQMAR 1950
PGGEGTDLPV GDWSRELAEA QRMMRDLRSR DFKKHLQEAE AEKMEAQLLL 2000
HRIRTWLESH QVENNGLLKN IRDSLNDYED KLQDLRSILQ EAAAQAKQAT 2050
GINHENEGVL GAIQRQMKEM DSLKNDFTKY LATADSSLLQ TNNLLQQMDK 2100
SQKEYESLAA ALNGARQELS DRVRELSRSG GKAPLVVEAE KHAQSLQELA 2150
KQLEEIKRNT SGDELVRCAV DAATAYENIL NAIRAAEDAA SKATSASKSA 2200
FQTVIKEDLP KRAKTLSSDS EELLNEAKMT QKRLQQVSPA LNSLQQTLKT 2250
VSVQKDLLDA NLTVARDDLH GIQRGDIDSV VIGAKSMVRE ANGITSEVLD 2300
GLNPIQTDLG RIKDSYESAR REDFSKALVD ANNSVKKLTR KLPDLFIKIE 2350
SINQQLLPLG NISDNVDRIR ELIQQARDAA NKVAIPMRFN GKSGVEVRLP 2400
NDLEDLKGYT SLSLFLQRPD LRENGGTEDM FVMYLGNKDA SKDYIGMAVV 2450
DGQLTCVYNL GDREAEVQID QVLTESESQE AVMDRVKFQR IYQFAKLNYT 2500
KEATSTKPKA PGVYDMESAS SNTLLNLDPE NAVFYVGGYP PGFELPRRLR 2550
FPPYKGCIEL DDLNENVLSL YNFKTTFNLN TTEVEPCRRR KEESDKNYFE 2600
GTGYARIPTQ PNAPFPNFMQ TIQTTVDRGL LFFAENQDNF ISLNIEDGNL 2650
MVKYKLNSEP PKEKGIRDTI NNGRDHMILI SIGKSQKRML INMNKHSIII 2700
EGEIFDFSTY YLGGIPIAIR ERFNISTPAF QGCMKNLKKT SGVVRLNDTV 2750
GVTKKCSEDW KLVRTASFSR GGQMSFTNLD VPSLDRFQLS FGFQTFQPSG 2800
TLLNHQTRTS SLLVTLEDGH IALSTRDSSS PIFKSPGTYM DGLLHHVSVI 2850
SDTSGLRLLI DDQVLRRNQR LASFSNAQQS LSMGGGYFEG CISNVFVQRM 2900
SQSPEVLDMA SKSTKRDAFL GGCSLNKPPF LMLFKSPKGF NKARSFNVNQ 2950
LLQDAPQAAR SIEAWQDGKS CLPPLNTKAT HRALQFGDSP TSHLLFKLPQ 3000
ELLKPRLQFS LDIQTTSSRG LVFHTGTRDS FVALYLSEGH VIFALGAGGK 3050
KLRLRSKERY HDGKWHSVVF GLSGRKVHLV VDGLRAQEGS LPGNSTISPR 3100
EQVYLGLSPS RKSKSLPQHS FVGCLRNFQL DSKPLDSPSA RSGVSPCLGG 3150
SLEKGIYFSQ GGGHVVLANS VSLEPALTLT LSIRPRSLTG VLIHIASQSG 3200
EHLSVYMEAG KVTTSMNSEA GGTVTSITPK RSLCDGQWHS VTVSIKQHTL 3250
HLELDTDNSY TAGQLSFPPN STRGSLHIGG VPDKLKMLTL PVWNSFFGCL 3300
KNIQVNHIPV PITEATDVQG SVSLNGCPDH 3330
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 16191619Missing in isoform A.
VSP_003038Add
BLAST
Alternative sequencei1620 – 166243FTETQ…TGDSC → MLPAVRWSAWSTGWLWIFGA ALGQCLGYGSEQQRVAFLQR PSQNHLQASYMELRPS in isoform A.
VSP_003039Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti982 – 9821A → R in CAA58837. 1 Publication
Sequence conflicti1150 – 11501W → R in CAA58837. 1 Publication
Sequence conflicti1224 – 12241E → K in CAA58837. 1 Publication
Sequence conflicti1272 – 12721G → GH in CAA58837. 1 Publication
Sequence conflicti1291 – 12911R → S in CAA58837. 1 Publication
Sequence conflicti1398 – 13981E → K in CAA58837. 1 Publication
Sequence conflicti1466 – 14661H → R in CAA58837. 1 Publication
Sequence conflicti1479 – 14791R → V in CAA58837. 1 Publication
Sequence conflicti1488 – 14881V → F in CAA58837. 1 Publication
Sequence conflicti1527 – 15282SS → II in CAA58837. 1 Publication
Sequence conflicti1608 – 16081S → P in CAA58837. 1 Publication
Sequence conflicti1983 – 19842KK → QN in CAA58836. 1 Publication
Sequence conflicti1983 – 19842KK → QN in CAA58837. 1 Publication
Sequence conflicti1983 – 19842KK → QN in AAA68091. 1 Publication
Sequence conflicti1987 – 19871Q → G in CAA58836. 1 Publication
Sequence conflicti1987 – 19871Q → G in CAA58837. 1 Publication
Sequence conflicti1987 – 19871Q → G in AAA68091. 1 Publication
Sequence conflicti2463 – 24631R → G in CAA58836. 1 Publication
Sequence conflicti2463 – 24631R → G in CAA58837. 1 Publication
Sequence conflicti2463 – 24631R → G in AAA68091. 1 Publication
Sequence conflicti2488 – 24881F → S in CAA58836. 1 Publication
Sequence conflicti2488 – 24881F → S in CAA58837. 1 Publication
Sequence conflicti2488 – 24881F → S in AAA68091. 1 Publication
Sequence conflicti2617 – 26204NFMQ → KLSW in CAA58836. 1 Publication
Sequence conflicti2617 – 26204NFMQ → KLSW in CAA58837. 1 Publication
Sequence conflicti2724 – 27252NI → PL in CAA58836. 1 Publication
Sequence conflicti2724 – 27252NI → PL in CAA58837. 1 Publication
Sequence conflicti3257 – 32571D → Y in CAA58836. 1 Publication
Sequence conflicti3257 – 32571D → Y in CAA58837. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
GeneIDi16774.
KEGGimmu:16774.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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...

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 ]
GeneIDi 16774.
KEGGi mmu:16774.

Organism-specific databases

CTDi 3909.
MGIi MGI:99909. Lama3.

Phylogenomic databases

eggNOGi NOG292643.
GeneTreei ENSGT00750000117549.
HOGENOMi HOG000048708.
HOVERGENi HBG052300.
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_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

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 IPR008985. 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 ]
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: September 3, 2014
This is version 136 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

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