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P19137 (LAMA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit alpha-1
Alternative name(s):
Laminin A chain
Laminin-1 subunit alpha
Laminin-3 subunit alpha
S-laminin subunit alpha
Short name=S-LAM alpha
Gene names
Name:Lama1
Synonyms:Lama, Lama-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3084 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.

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-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Domain

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

Domains VI, IV and G are globular.

Sequence similarities

Contains 17 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 2 laminin IV type A domains.

Contains 1 laminin N-terminal domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 11798066. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface receptor signaling pathway

Inferred from direct assay PubMed 11827968. Source: MGI

epithelial tube branching involved in lung morphogenesis

Inferred from mutant phenotype PubMed 11798066PubMed 1907584. Source: MGI

establishment of epithelial cell apical/basal polarity

Inferred from mutant phenotype PubMed 15668394. Source: MGI

morphogenesis of an epithelial sheet

Inferred from mutant phenotype PubMed 11798066PubMed 15668394. Source: MGI

neuron projection development

Inferred from direct assay PubMed 19118221. Source: MGI

regulation of cell adhesion

Inferred from electronic annotation. Source: InterPro

regulation of cell migration

Inferred from electronic annotation. Source: InterPro

regulation of embryonic development

Inferred from electronic annotation. Source: InterPro

retina development in camera-type eye

Inferred from mutant phenotype PubMed 21052544. Source: MGI

retinal blood vessel morphogenesis

Inferred from mutant phenotype PubMed 21052544. Source: MGI

tissue development

Inferred from mutant phenotype PubMed 15102706. Source: MGI

   Cellular_componentbasal lamina

Traceable author statement PubMed 8995276. Source: MGI

basement membrane

Inferred from direct assay PubMed 12631063PubMed 16631359. Source: UniProtKB

cell-cell junction

Inferred from direct assay PubMed 19319192PubMed 19531352PubMed 20123909PubMed 21131290. Source: MGI

extracellular matrix

Inferred from direct assay PubMed 15065125PubMed 1907584PubMed 7589890. Source: MGI

extracellular region

Traceable author statement. Source: Reactome

laminin complex

Inferred from direct assay PubMed 8034675. Source: MGI

laminin-1 complex

Inferred from direct assay PubMed 17517882PubMed 9264260. Source: MGI

proteinaceous extracellular matrix

Inferred from direct assay PubMed 11984530PubMed 14697343PubMed 16554364. Source: MGI

   Molecular_functionextracellular matrix structural constituent

Inferred from direct assay PubMed 11984530. Source: MGI

glycosphingolipid binding

Inferred from direct assay PubMed 19118221. Source: MGI

protein binding

Inferred from physical interaction PubMed 16709410. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DAG1O187382EBI-7176628,EBI-8522926From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.4
Chain25 – 30843060Laminin subunit alpha-1
PRO_0000017055

Regions

Domain25 – 276252Laminin N-terminal
Domain277 – 33357Laminin EGF-like 1
Domain334 – 40370Laminin EGF-like 2
Domain404 – 46057Laminin EGF-like 3
Domain461 – 50949Laminin EGF-like 4
Domain510 – 51910Laminin EGF-like 5; first part
Domain523 – 715193Laminin IV type A 1
Domain716 – 74833Laminin EGF-like 5; second part
Domain749 – 79749Laminin EGF-like 6
Domain798 – 85558Laminin EGF-like 7
Domain856 – 90853Laminin EGF-like 8
Domain909 – 95749Laminin EGF-like 9
Domain958 – 100447Laminin EGF-like 10
Domain1005 – 105046Laminin EGF-like 11
Domain1051 – 109646Laminin EGF-like 12
Domain1097 – 115660Laminin EGF-like 13
Domain1157 – 116610Laminin EGF-like 14; first part
Domain1177 – 1368192Laminin IV type A 2
Domain1369 – 140941Laminin EGF-like 14; second part
Domain1410 – 145849Laminin EGF-like 15
Domain1459 – 151557Laminin EGF-like 16
Domain1516 – 156247Laminin EGF-like 17
Domain2125 – 2305181Laminin G-like 1
Domain2313 – 2489177Laminin G-like 2
Domain2494 – 2680187Laminin G-like 3
Domain2722 – 2894173Laminin G-like 4
Domain2899 – 3079181Laminin G-like 5
Region1564 – 2124561Domain II and I
Coiled coil1612 – 1820209 Potential
Coiled coil1869 – 190335 Potential
Coiled coil2096 – 212833 Potential
Motif1147 – 11493Cell attachment site

Amino acid modifications

Modified residue251Pyrrolidone carboxylic acid
Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5621N-linked (GlcNAc...) Potential
Glycosylation6721N-linked (GlcNAc...) Potential
Glycosylation7701N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...) Potential
Glycosylation9141N-linked (GlcNAc...) Potential
Glycosylation9591N-linked (GlcNAc...) Potential
Glycosylation9691N-linked (GlcNAc...) Potential
Glycosylation10521N-linked (GlcNAc...) Potential
Glycosylation13441N-linked (GlcNAc...) Ref.6
Glycosylation14141N-linked (GlcNAc...) Potential
Glycosylation15861N-linked (GlcNAc...) Potential
Glycosylation16031N-linked (GlcNAc...) Potential
Glycosylation16591N-linked (GlcNAc...) Potential
Glycosylation16861N-linked (GlcNAc...) Ref.6
Glycosylation17061N-linked (GlcNAc...) Potential
Glycosylation17181N-linked (GlcNAc...) Ref.6
Glycosylation17251N-linked (GlcNAc...) Ref.6
Glycosylation17631N-linked (GlcNAc...) Ref.6
Glycosylation18121N-linked (GlcNAc...) Potential
Glycosylation19021N-linked (GlcNAc...) Potential
Glycosylation19061N-linked (GlcNAc...) Potential
Glycosylation19361N-linked (GlcNAc...) Ref.6
Glycosylation19821N-linked (GlcNAc...) Potential
Glycosylation19931N-linked (GlcNAc...) Potential
Glycosylation19991N-linked (GlcNAc...) Potential
Glycosylation20271N-linked (GlcNAc...) Ref.6
Glycosylation20461N-linked (GlcNAc...) Ref.6
Glycosylation20551N-linked (GlcNAc...) Potential
Glycosylation20621N-linked (GlcNAc...); atypical Ref.6
Glycosylation20671N-linked (GlcNAc...) Ref.6
Glycosylation21021N-linked (GlcNAc...) Potential
Glycosylation21061N-linked (GlcNAc...) Potential
Glycosylation22511N-linked (GlcNAc...) Potential
Glycosylation22521N-linked (GlcNAc...) Potential
Glycosylation23561N-linked (GlcNAc...) Potential
Glycosylation23921N-linked (GlcNAc...) Potential
Glycosylation25261N-linked (GlcNAc...) Potential
Glycosylation27381N-linked (GlcNAc...) Potential
Glycosylation28351N-linked (GlcNAc...) Ref.6
Glycosylation29241N-linked (GlcNAc...) Potential
Disulfide bond277 ↔ 286 By similarity
Disulfide bond279 ↔ 297 By similarity
Disulfide bond299 ↔ 308 By similarity
Disulfide bond311 ↔ 331 By similarity
Disulfide bond334 ↔ 343 By similarity
Disulfide bond336 ↔ 368 By similarity
Disulfide bond371 ↔ 380 By similarity
Disulfide bond383 ↔ 401 By similarity
Disulfide bond404 ↔ 416 By similarity
Disulfide bond406 ↔ 434 By similarity
Disulfide bond436 ↔ 445 By similarity
Disulfide bond448 ↔ 458 By similarity
Disulfide bond461 ↔ 474 By similarity
Disulfide bond463 ↔ 478 By similarity
Disulfide bond480 ↔ 489 By similarity
Disulfide bond492 ↔ 507 By similarity
Disulfide bond749 ↔ 758 By similarity
Disulfide bond751 ↔ 764 By similarity
Disulfide bond767 ↔ 776 By similarity
Disulfide bond779 ↔ 795 By similarity
Disulfide bond798 ↔ 813 By similarity
Disulfide bond800 ↔ 823 By similarity
Disulfide bond826 ↔ 835 By similarity
Disulfide bond838 ↔ 853 By similarity
Disulfide bond856 ↔ 870 By similarity
Disulfide bond858 ↔ 877 By similarity
Disulfide bond880 ↔ 889 By similarity
Disulfide bond892 ↔ 906 By similarity
Disulfide bond909 ↔ 921 By similarity
Disulfide bond911 ↔ 928 By similarity
Disulfide bond930 ↔ 939 By similarity
Disulfide bond942 ↔ 955 By similarity
Disulfide bond958 ↔ 970 By similarity
Disulfide bond960 ↔ 976 By similarity
Disulfide bond978 ↔ 987 By similarity
Disulfide bond990 ↔ 1002 By similarity
Disulfide bond1005 ↔ 1014 By similarity
Disulfide bond1007 ↔ 1021 By similarity
Disulfide bond1023 ↔ 1032 By similarity
Disulfide bond1035 ↔ 1048 By similarity
Disulfide bond1051 ↔ 1063 By similarity
Disulfide bond1053 ↔ 1070 By similarity
Disulfide bond1072 ↔ 1081 By similarity
Disulfide bond1084 ↔ 1094 By similarity
Disulfide bond1097 ↔ 1109 By similarity
Disulfide bond1099 ↔ 1125 By similarity
Disulfide bond1127 ↔ 1136 By similarity
Disulfide bond1139 ↔ 1154 By similarity
Disulfide bond1410 ↔ 1419 By similarity
Disulfide bond1412 ↔ 1426 By similarity
Disulfide bond1429 ↔ 1438 By similarity
Disulfide bond1441 ↔ 1456 By similarity
Disulfide bond1459 ↔ 1473 By similarity
Disulfide bond1461 ↔ 1483 By similarity
Disulfide bond1486 ↔ 1495 By similarity
Disulfide bond1498 ↔ 1513 By similarity
Disulfide bond1516 ↔ 1528 By similarity
Disulfide bond1518 ↔ 1535 By similarity
Disulfide bond1537 ↔ 1546 By similarity
Disulfide bond1549 ↔ 1560 By similarity
Disulfide bond1563Interchain Probable
Disulfide bond1567Interchain Probable
Disulfide bond2279 ↔ 2305 By similarity
Disulfide bond2465 ↔ 2489 By similarity
Disulfide bond2653 ↔ 2680 By similarity
Disulfide bond2869 ↔ 2894 By similarity
Disulfide bond3048 ↔ 3079 By similarity

Experimental info

Sequence conflict2091I → T Ref.2

Secondary structure

.......................................................... 3084
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19137 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: CF8E0D508046FC23

FASTA3,084338,172
        10         20         30         40         50         60 
MRGSGTGAAL LVLLASVLWV TVRSQQRGLF PAILNLATNA HISANATCGE KGPEMFCKLV 

        70         80         90        100        110        120 
EHVPGRPVRH AQCRVCDGNS TNPRERHPIS HAIDGTNNWW QSPSIQNGRE YHWVTVTLDL 

       130        140        150        160        170        180 
RQVFQVAYII IKAANAPRPG NWILERSVDG VKFKPWQYYA VSDTECLTRY KITPRRGPPT 

       190        200        210        220        230        240 
YRADNEVICT SYYSKLVPLE HGEIHTSLIN GRPSADDPSP QLLEFTSARY IRLRLQRIRT 

       250        260        270        280        290        300 
LNADLMTLSH RDLRDLDPIV TRRYYYSIKD ISVGGMCICY GHASSCPWDE EAKQLQCQCE 

       310        320        330        340        350        360 
HNTCGESCDR CCPGYHQQPW RPGTISSGNE CEECNCHNKA KDCYYDSSVA KERRSLNTAG 

       370        380        390        400        410        420 
QYSGGGVCVN CSQNTTGINC ETCIDQYYRP HKVSPYDDHP CRPCNCDPVG SLSSVCIKDD 

       430        440        450        460        470        480 
RHADLANGKW PGQCPCRKGY AGDKCDRCQF GYRGFPNCIP CDCRTVGSLN EDPCIEPCLC 

       490        500        510        520        530        540 
KKNVEGKNCD RCKPGFYNLK ERNPEGCSEC FCFGVSGVCD SLTWSISQVT NMSGWLVTDL 

       550        560        570        580        590        600 
MSTNKIRSQQ DVLGGHRQIS INNTAVMQRL TSTYYWAAPE AYLGNKLTAF GGFLKYTVSY 

       610        620        630        640        650        660 
DIPVETVDSD LMSHADIIIK GNGLTISTRA EGLSLQPYEE YFNVVRLVPE NFRDFNTRRE 

       670        680        690        700        710        720 
IDRDQLMTVL ANVTHLLIRA NYNSAKMALY RLDSVSLDIA SPNAIDLAVA ADVEHCECPQ 

       730        740        750        760        770        780 
GYTGTSCEAC LPGYYRVDGI LFGGICQPCE CHGHASECDI HGICSVCTHN TTGDHCEQCL 

       790        800        810        820        830        840 
PGFYGTPSRG TPGDCQPCAC PLSIDSNNFS PTCHLTDGEE VVCDQCAPGY SGSWCERCAD 

       850        860        870        880        890        900 
GYYGNPTVPG GTCVPCNCSG NVDPLEAGHC DSVTGECLKC LWNTDGAHCE RCADGFYGDA 

       910        920        930        940        950        960 
VTAKNCRACD CHENGSLSGV CHLETGLCDC KPHVTGQQCD QCLSGYYGLD TGLGCVPCNC 

       970        980        990       1000       1010       1020 
SVEGSVSDNC TEEGQCHCGP GVSGKQCDRC SHGFYAFQDG GCTPCDCAHT QNNCDPASGE 

      1030       1040       1050       1060       1070       1080 
CLCPPHTQGL KCEECEEAYW GLDPEQGCQA CNCSAVGSTS AQCDVLSGHC PCKKGFGGQS 

      1090       1100       1110       1120       1130       1140 
CHQCSLGYRS FPDCVPCGCD LRGTLPDTCD LEQGLCSCSE DSGTCSCKEN VVGPQCSKCQ 

      1150       1160       1170       1180       1190       1200 
AGTFALRGDN PQGCSPCFCF GLSQLCSELE GYVRTLITLA SDQPLLHVVS QSNLKGTIEG 

      1210       1220       1230       1240       1250       1260 
VHFQPPDTLL DAEAVRQHIY AEPFYWRLPK QFQGDQLLAY GGKLQYSVAF YSTLGTGTSN 

      1270       1280       1290       1300       1310       1320 
YEPQVLIKGG RARKHVIYMD APAPENGVRQ DYEVQMKEEF WKYFNSVSEK HVTHSDFMSV 

      1330       1340       1350       1360       1370       1380 
LSNIDYILIK ASYGQGLQQS RIANISMEVG RKAVELPAEG EAALLLELCV CPPGTAGHSC 

      1390       1400       1410       1420       1430       1440 
QDCAPGYYRE KLPESGGRGP RPLLAPCVPC NCNNHSDVCD PETGKCLSCR DHTSGDHCEL 

      1450       1460       1470       1480       1490       1500 
CASGYYGKVT GLPGDCTPCT CPHHPPFSFS PTCVVEGDSD FRCNACLPGY EGQYCERCSA 

      1510       1520       1530       1540       1550       1560 
GYHGNPRAAG GSCQTCDCNP QGSVHSDCDR ASGQCVCKPG ATGLHCEKCL PRHILMESDC 

      1570       1580       1590       1600       1610       1620 
VSCDDDCVGP LLNDLDSVGD AVLSLNLTGV SPAPYGILEN LENTTKYFQR YLIKENAKKI 

      1630       1640       1650       1660       1670       1680 
RAEIQLEGIA EQTENLQKEL TRVLARHQKV NAEMERTSNG TQALATFIEQ LHANIKEITE 

      1690       1700       1710       1720       1730       1740 
KVATLNQTAR KDFQPPVSAL QSMHQNISSL LGLIKERNFT EMQQNATLEL KAAKDLLSRI 

      1750       1760       1770       1780       1790       1800 
QKRFQKPQEK LKALKEANSL LSNHSEKLQA AEELLKEAGS KTQESNLLLL LVKANLKEEF 

      1810       1820       1830       1840       1850       1860 
QEKKLRVQEE QNVTSELIAK GREWVDAAGT HTAAAQDTLT QLEHHRDELL LWARKIRSHV 

      1870       1880       1890       1900       1910       1920 
DDLVMQMSKR RARDLVHRAE QHASELQSRA GALDRDLENV RNVSLNATSA AHVHSNIQTL 

      1930       1940       1950       1960       1970       1980 
TEEAEMLAAD AHKTANKTDL ISESLASRGK AVLQRSSRFL KESVGTRRKQ QGITMKLDEL 

      1990       2000       2010       2020       2030       2040 
KNLTSQFQES VDNITKQAND SLAMLRESPG GMREKGRKAR ELAAAANESA VKTLEDVLAL 

      2050       2060       2070       2080       2090       2100 
SLRVFNTSED LSRVNATVQE TNDLLHNSTM TTLLAGRKMK DMEMQANLLL DRLKPLKTLE 

      2110       2120       2130       2140       2150       2160 
ENLSRNLSEI KLLISRARKQ AASIKVAVSA DRDCIRAYQP QTSSTNYNTL ILNVKTQEPD 

      2170       2180       2190       2200       2210       2220 
NLLFYLGSSS SSDFLAVEMR RGKVAFLWDL GSGSTRLEFP EVSINNNRWH SIYITRFGNM 

      2230       2240       2250       2260       2270       2280 
GSLSVKEASA AENPPVRTSK SPGPSKVLDI NNSTLMFVGG LGGQIKKSPA VKVTHFKGCM 

      2290       2300       2310       2320       2330       2340 
GEAFLNGKSI GLWNYIEREG KCNGCFGSSQ NEDSSFHFDG SGYAMVEKTL RPTVTQIVIL 

      2350       2360       2370       2380       2390       2400 
FSTFSPNGLL FYLASNGTKD FLSIELVRGR VKVMVDLGSG PLTLMTDRRY NNGTWYKIAF 

      2410       2420       2430       2440       2450       2460 
QRNRKQGLLA VFDAYDTSDK ETKQGETPGA ASDLNRLEKD LIYVGGLPHS KAVRKGVSSR 

      2470       2480       2490       2500       2510       2520 
SYVGCIKNLE ISRSTFDLLR NSYGVRKGCA LEPIQSVSFL RGGYVEMPPK SLSPESSLLA 

      2530       2540       2550       2560       2570       2580 
TFATKNSSGI LLVALGKDAE EAGGAQAHVP FFSIMLLEGR IEVHVNSGDG TSLRKALLHA 

      2590       2600       2610       2620       2630       2640 
PTGSYSDGQE HSISLVRNRR VITIQVDENS PVEMKLGPLT EGKTIDISNL YIGGLPEDKA 

      2650       2660       2670       2680       2690       2700 
TPMLKMRTSF HGCIKNVVLD AQLLDFTHAT GSEQVELDTC LLAEEPMQSL HREHGELPPE 

      2710       2720       2730       2740       2750       2760 
PPTLPQPELC AVDTAPGYVA GAHQFGLSQN SHLVLPLNQS DVRKRLQVQL SIRTFASSGL 

      2770       2780       2790       2800       2810       2820 
IYYVAHQNQM DYATLQLQEG RLHFMFDLGK GRTKVSHPAL LSDGKWHTVK TEYIKRKAFM 

      2830       2840       2850       2860       2870       2880 
TVDGQESPSV TVVGNATTLD VERKLYLGGL PSHYRARNIG TITHSIPACI GEIMVNGQQL 

      2890       2900       2910       2920       2930       2940 
DKDRPLSASA VDRCYVVAQE GTFFEGSGYA ALVKEGYKVR LDLNITLEFR TTSKNGVLLG 

      2950       2960       2970       2980       2990       3000 
ISSAKVDAIG LEIVDGKVLF HVNNGAGRIT ATYQPRAARA LCDGKWHTLQ AHKSKHRIVL 

      3010       3020       3030       3040       3050       3060 
TVDGNSVRAE SPHTHSTSAD TNDPIYVGGY PAHIKQNCLS SRASFRGCVR NLRLSRGSQV 

      3070       3080 
QSLDLSRAFD LQGVFPHSCP GPEP 

« Hide

References

« Hide 'large scale' references
[1]"Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains."
Sasaki M., Kleinman H.K., Huber H., Deutzmann R., Yamada Y.
J. Biol. Chem. 263:16536-16544(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The N-terminus of laminin A chain is homologous to the B chains."
Hartl L., Oberbaeumer I., Deutzmann R.
Eur. J. Biochem. 173:629-635(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-339.
[3]"Structural study of long arm fragments of laminin. Evidence for repetitive C-terminal sequences in the A-chain, not present in the B-chains."
Deutzmann R., Huber J., Schmetz K.A., Oberbaeumer I., Hartl L.
Eur. J. Biochem. 177:35-45(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2538-3084, PARTIAL PROTEIN SEQUENCE.
[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: PROTEIN SEQUENCE OF 25-32, PYROGLUTAMATE FORMATION AT GLN-25.
[5]"Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands."
Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.
Eur. J. Biochem. 215:733-740(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLN1.
[6]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1344; ASN-1686; ASN-1718; ASN-1725; ASN-1763; ASN-1936; ASN-2027; ASN-2046; ASN-2062; ASN-2067 AND ASN-2835.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04064 mRNA. Translation: AAA39410.1.
X07737 mRNA. Translation: CAA30561.1.
X13459 mRNA. Translation: CAA31807.1.
M36775 mRNA. Translation: AAA39406.1.
PIRMMMSA. A31771.
RefSeqNP_032506.2. NM_008480.2.
UniGeneMm.303386.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JD4X-ray1.90A/B2706-3084[»]
ProteinModelPortalP19137.
SMRP19137. Positions 29-523, 715-1154, 1369-1558, 2140-3083.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201096. 7 interactions.
IntActP19137. 4 interactions.
MINTMINT-2635122.
STRING10090.ENSMUSP00000043957.

PTM databases

PhosphoSiteP19137.

Proteomic databases

MaxQBP19137.
PaxDbP19137.
PRIDEP19137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16772.
KEGGmmu:16772.

Organism-specific databases

CTD284217.
MGIMGI:99892. Lama1.

Phylogenomic databases

eggNOGNOG247347.
HOGENOMHOG000293201.
HOVERGENHBG052298.
InParanoidP19137.
KOK05637.
PhylomeDBP19137.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
REACT_206066. Extracellular matrix organization.

Gene expression databases

CleanExMM_LAMA1.
GenevestigatorP19137.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR013032. EGF-like_CS.
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. 2 hits.
PF00053. Laminin_EGF. 17 hits.
PF00054. Laminin_G_1. 4 hits.
PF02210. Laminin_G_2. 1 hit.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 5 hits.
PROSITEPS00022. EGF_1. 11 hits.
PS01186. EGF_2. 3 hits.
PS01248. EGF_LAM_1. 15 hits.
PS50027. EGF_LAM_2. 15 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 2 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19137.
NextBio290602.
PROP19137.
SOURCESearch...

Entry information

Entry nameLAMA1_MOUSE
AccessionPrimary (citable) accession number: P19137
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 11, 2014
This is version 151 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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