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Protein

Laminin subunit alpha-1

Gene

Lama1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-3000157 Laminin interactions
R-MMU-8874081 MET activates PTK2 signaling

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Lama1
Synonyms:Lama, Lama-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:99892 Lama1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001705525 – 3083Laminin subunit alpha-1Add BLAST3059

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi277 ↔ 286PROSITE-ProRule annotation
Disulfide bondi279 ↔ 297PROSITE-ProRule annotation
Disulfide bondi299 ↔ 308PROSITE-ProRule annotation
Disulfide bondi311 ↔ 331PROSITE-ProRule annotation
Disulfide bondi334 ↔ 343PROSITE-ProRule annotation
Disulfide bondi336 ↔ 368PROSITE-ProRule annotation
Glycosylationi370N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi371 ↔ 380PROSITE-ProRule annotation
Disulfide bondi383 ↔ 401PROSITE-ProRule annotation
Disulfide bondi404 ↔ 416PROSITE-ProRule annotation
Disulfide bondi406 ↔ 434PROSITE-ProRule annotation
Disulfide bondi436 ↔ 445PROSITE-ProRule annotation
Disulfide bondi448 ↔ 458PROSITE-ProRule annotation
Disulfide bondi461 ↔ 474PROSITE-ProRule annotation
Disulfide bondi463 ↔ 478PROSITE-ProRule annotation
Disulfide bondi480 ↔ 489PROSITE-ProRule annotation
Disulfide bondi492 ↔ 507PROSITE-ProRule annotation
Glycosylationi672N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi749 ↔ 758PROSITE-ProRule annotation
Disulfide bondi751 ↔ 764PROSITE-ProRule annotation
Disulfide bondi767 ↔ 776PROSITE-ProRule annotation
Disulfide bondi779 ↔ 795PROSITE-ProRule annotation
Disulfide bondi798 ↔ 813PROSITE-ProRule annotation
Disulfide bondi800 ↔ 823PROSITE-ProRule annotation
Disulfide bondi826 ↔ 835PROSITE-ProRule annotation
Disulfide bondi838 ↔ 853PROSITE-ProRule annotation
Disulfide bondi856 ↔ 870PROSITE-ProRule annotation
Disulfide bondi858 ↔ 877PROSITE-ProRule annotation
Disulfide bondi880 ↔ 889PROSITE-ProRule annotation
Disulfide bondi892 ↔ 906PROSITE-ProRule annotation
Disulfide bondi909 ↔ 921PROSITE-ProRule annotation
Disulfide bondi911 ↔ 928PROSITE-ProRule annotation
Disulfide bondi930 ↔ 939PROSITE-ProRule annotation
Disulfide bondi942 ↔ 955PROSITE-ProRule annotation
Disulfide bondi958 ↔ 970PROSITE-ProRule annotation
Disulfide bondi960 ↔ 976PROSITE-ProRule annotation
Disulfide bondi978 ↔ 987PROSITE-ProRule annotation
Disulfide bondi990 ↔ 1002PROSITE-ProRule annotation
Disulfide bondi1005 ↔ 1014PROSITE-ProRule annotation
Disulfide bondi1007 ↔ 1021PROSITE-ProRule annotation
Disulfide bondi1023 ↔ 1032PROSITE-ProRule annotation
Disulfide bondi1035 ↔ 1048PROSITE-ProRule annotation
Disulfide bondi1051 ↔ 1063PROSITE-ProRule annotation
Disulfide bondi1053 ↔ 1070PROSITE-ProRule annotation
Disulfide bondi1072 ↔ 1081PROSITE-ProRule annotation
Disulfide bondi1084 ↔ 1094PROSITE-ProRule annotation
Disulfide bondi1097 ↔ 1109PROSITE-ProRule annotation
Disulfide bondi1099 ↔ 1125PROSITE-ProRule annotation
Disulfide bondi1127 ↔ 1136PROSITE-ProRule annotation
Disulfide bondi1139 ↔ 1154PROSITE-ProRule annotation
Glycosylationi1344N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi1410 ↔ 1419PROSITE-ProRule annotation
Disulfide bondi1412 ↔ 1426PROSITE-ProRule annotation
Disulfide bondi1429 ↔ 1438PROSITE-ProRule annotation
Disulfide bondi1441 ↔ 1456PROSITE-ProRule annotation
Disulfide bondi1459 ↔ 1473PROSITE-ProRule annotation
Disulfide bondi1461 ↔ 1483PROSITE-ProRule annotation
Disulfide bondi1486 ↔ 1495PROSITE-ProRule annotation
Disulfide bondi1498 ↔ 1513PROSITE-ProRule annotation
Disulfide bondi1516 ↔ 1528PROSITE-ProRule annotation
Disulfide bondi1518 ↔ 1535PROSITE-ProRule annotation
Disulfide bondi1537 ↔ 1546PROSITE-ProRule annotation
Disulfide bondi1549 ↔ 1560PROSITE-ProRule annotation
Disulfide bondi1563InterchainCurated
Disulfide bondi1567InterchainCurated
Glycosylationi1659N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1686N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1718N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1725N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1763N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1811N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1935N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi2026N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi2045N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi2066N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi2278 ↔ 2304PROSITE-ProRule annotation
Glycosylationi2355N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2464 ↔ 2488PROSITE-ProRule annotation
Disulfide bondi2652 ↔ 2679PROSITE-ProRule annotation
Glycosylationi2834N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi2868 ↔ 2893PROSITE-ProRule annotation
Glycosylationi2923N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3047 ↔ 3078PROSITE-ProRule annotation

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP19137
PaxDbiP19137
PeptideAtlasiP19137
PRIDEiP19137

PTM databases

iPTMnetiP19137
PhosphoSitePlusiP19137

Expressioni

Gene expression databases

BgeeiENSMUSG00000032796 Expressed in 228 organ(s), highest expression level in maturing glomerular tuft (mouse)
CleanExiMM_LAMA1
GenevisibleiF8VQ40 MM

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

Binary interactionsi

WithEntry#Exp.IntActNotes
DAG1O187382EBI-7176628,EBI-8522926From Bos taurus.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201096, 8 interactors
ComplexPortaliCPX-3008 Laminin-111 complex
CPX-3010 Laminin-121 complex
IntActiP19137, 5 interactors
MINTiP19137
STRINGi10090.ENSMUSP00000043957

Structurei

Secondary structure

13083
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP19137
SMRiP19137
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19137

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 276Laminin N-terminalPROSITE-ProRule annotationAdd BLAST252
Domaini277 – 333Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST57
Domaini334 – 403Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini404 – 460Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST57
Domaini461 – 509Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST49
Domaini510 – 519Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini523 – 715Laminin IV type A 1PROSITE-ProRule annotationAdd BLAST193
Domaini716 – 748Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST33
Domaini749 – 797Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST49
Domaini798 – 855Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST58
Domaini856 – 908Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST53
Domaini909 – 957Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST49
Domaini958 – 1004Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST47
Domaini1005 – 1050Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST46
Domaini1051 – 1096Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST46
Domaini1097 – 1156Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST60
Domaini1157 – 1166Laminin EGF-like 14; first partPROSITE-ProRule annotation10
Domaini1177 – 1368Laminin IV type A 2PROSITE-ProRule annotationAdd BLAST192
Domaini1369 – 1409Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd BLAST41
Domaini1410 – 1458Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST49
Domaini1459 – 1515Laminin EGF-like 16PROSITE-ProRule annotationAdd BLAST57
Domaini1516 – 1562Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST47
Domaini2124 – 2304Laminin G-like 1PROSITE-ProRule annotationAdd BLAST181
Domaini2312 – 2488Laminin G-like 2PROSITE-ProRule annotationAdd BLAST177
Domaini2493 – 2679Laminin G-like 3PROSITE-ProRule annotationAdd BLAST187
Domaini2721 – 2893Laminin G-like 4PROSITE-ProRule annotationAdd BLAST173
Domaini2898 – 3078Laminin G-like 5PROSITE-ProRule annotationAdd BLAST181

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1564 – 2123Domain II and IAdd BLAST560

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1617 – 1691Sequence analysisAdd BLAST75
Coiled coili1723 – 1809Sequence analysisAdd BLAST87
Coiled coili1868 – 1901Sequence analysisAdd BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1147 – 1149Cell attachment site3

Domaini

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.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1836 Eukaryota
ENOG410XRDC LUCA
GeneTreeiENSGT00780000121851
HOGENOMiHOG000293201
HOVERGENiHBG052298
InParanoidiP19137
KOiK05637
OMAiICQPCEC
OrthoDBiEOG091G005L
PhylomeDBiP19137
TreeFamiTF335359

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR009254 Laminin_aI
IPR010307 Laminin_dom_II
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000034 Laminin_IV
IPR008211 Laminin_N
IPR038684 Laminin_N_sf
PfamiView protein in Pfam
PF00052 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
SMARTiView protein in SMART
SM00181 EGF, 10 hits
SM00180 EGF_Lam, 16 hits
SM00281 LamB, 2 hits
SM00282 LamG, 5 hits
SM00136 LamNT, 1 hit
SUPFAMiSSF49899 SSF49899, 5 hits
PROSITEiView protein in PROSITE
PS00022 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

Sequencei

Sequence statusi: Complete.

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

P19137-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRGSGTGAAL LVLLASVLWV TVRSQQRGLF PAILNLATNA HISANATCGE
60 70 80 90 100
KGPEMFCKLV EHVPGRPVRH AQCRVCDGNS TNPRERHPIS HAIDGTNNWW
110 120 130 140 150
QSPSIQNGRE YHWVTVTLDL RQVFQVAYII IKAANAPRPG NWILERSVDG
160 170 180 190 200
VKFKPWQYYA VSDTECLTRY KITPRRGPPT YRADNEVICT SYYSKLVPLE
210 220 230 240 250
HGEIHTSLIN GRPSADDPSP QLLEFTSARY IRLRLQRIRT LNADLMTLSH
260 270 280 290 300
RDLRDLDPIV TRRYYYSIKD ISVGGMCICY GHASSCPWDE EAKQLQCQCE
310 320 330 340 350
HNTCGESCDR CCPGYHQQPW RPGTISSGNE CEECNCHNKA KDCYYDSSVA
360 370 380 390 400
KERRSLNTAG QYSGGGVCVN CSQNTTGINC ETCIDQYYRP HKVSPYDDHP
410 420 430 440 450
CRPCNCDPVG SLSSVCIKDD RHADLANGKW PGQCPCRKGY AGDKCDRCQF
460 470 480 490 500
GYRGFPNCIP CDCRTVGSLN EDPCIEPCLC KKNVEGKNCD RCKPGFYNLK
510 520 530 540 550
ERNPEGCSEC FCFGVSGVCD SLTWSISQVT NMSGWLVTDL MSTNKIRSQQ
560 570 580 590 600
DVLGGHRQIS INNTAVMQRL TSTYYWAAPE AYLGNKLTAF GGFLKYTVSY
610 620 630 640 650
DIPVETVDSD LMSHADIIIK GNGLTISTRA EGLSLQPYEE YFNVVRLVPE
660 670 680 690 700
NFRDFDTRRE IDRDQLMTVL ANVTHLLIRA NYNSAKMALY RLDSVSLDIA
710 720 730 740 750
SPNAIDLAVA ADVEHCECPQ GYTGTSCEAC LPGYYRVDGI LFGGICQPCE
760 770 780 790 800
CHGHASECDI HGICSVCTHN TTGDHCEQCL PGFYGTPSRG TPGDCQPCAC
810 820 830 840 850
PLSIDSNNFS PTCHLTDGEE VVCDQCAPGY SGSWCERCAD GYYGNPTVPG
860 870 880 890 900
GTCVPCNCSG NVDPLEAGHC DSVTGECLKC LWNTDGAHCE RCADGFYGDA
910 920 930 940 950
VTAKNCRACD CHENGSLSGI CHLETGLCDC KPHVTGQQCD QCLSGYYGLD
960 970 980 990 1000
TGLGCVPCNC SVEGSVSDNC TEEGQCHCGP GVSGKQCDRC SHGFYAFQDG
1010 1020 1030 1040 1050
GCTPCDCAHT QNNCDPASGE CLCPPHTQGL KCEECEEAYW GLDPEQGCQA
1060 1070 1080 1090 1100
CNCSAVGSTS AQCDVLSGHC PCKKGFGGQS CHQCSLGYRS FPDCVPCGCD
1110 1120 1130 1140 1150
LRGTLPDTCD LEQGLCSCSE DGGTCSCKEN AVGPQCSKCQ AGTFALRGDN
1160 1170 1180 1190 1200
PQGCSPCFCF GLSQLCSELE GYVRTLITLA SDQPLLHVVS QSNLKGTIEG
1210 1220 1230 1240 1250
VHFQPPDTLL DAEAVRQHIY AEPFYWRLPK QFQGDQLLAY GGKLQYSVAF
1260 1270 1280 1290 1300
YSTLGTGTSN YEPQVLIKGG RARKHVIYMD APAPENGVRQ DYEVRMKEEF
1310 1320 1330 1340 1350
WKYFNSVSEK HVTHSDFMSV LSNIDYILIK ASYGQGLQQS RIANISMEVG
1360 1370 1380 1390 1400
RKAVELPAEG EAALLLELCV CPPGTAGHSC QDCAPGYYRE KLPESGGRGP
1410 1420 1430 1440 1450
RPLLAPCVPC NCNNHSDVCD PETGKCLSCR DHTSGDHCEL CASGYYGKVT
1460 1470 1480 1490 1500
GLPGDCTPCT CPHHPPFSFS PTCVVEGDSD FRCNACLPGY EGQYCERCSA
1510 1520 1530 1540 1550
GYHGNPRAAG GSCQTCDCNP QGSVHSDCDR ASGQCVCKPG ATGLHCEKCL
1560 1570 1580 1590 1600
PRHILMESDC VSCDDDCVGP LLNDLDSVGD AVLSLNLTGV SPAPYGILEN
1610 1620 1630 1640 1650
LENTTKYFQR YLIKENAKKI RAEIQLEGIA EQTENLQKEL TRVLARHQKV
1660 1670 1680 1690 1700
NAEMERTSNG TQALATFIEQ LHANIKEITE KVATLNQTAR KDFQPPVSAL
1710 1720 1730 1740 1750
QSMHQNISSL LGLIKERNFT EMQQNATLEL KAAKDLLSRI QKRFQKPQEK
1760 1770 1780 1790 1800
LKALKEANSL LSNHSEKLQA AEELLKEAGS KTQESNLLLL LVKANLKEFQ
1810 1820 1830 1840 1850
EKKLRVQEEQ NVTSELIAKG REWVDAAGTH TAAAQDTLTQ LEHHRDELLL
1860 1870 1880 1890 1900
WARKIRSHVD DLVMQMSKRR ARDLVHRAEQ HASELQSRAG ALDRDLENVR
1910 1920 1930 1940 1950
NVSLNATSAA HVHSNIQTLT EEAEMLAADA HKTANKTDLI SESLASRGKA
1960 1970 1980 1990 2000
VLQRSSRFLK ESVSTRRKQQ GITMKLDELK NLTSQFQESM DNIMKQANDS
2010 2020 2030 2040 2050
LAMLRESPGG MREKGRKARE LAAAANESAV KTLEDVLALS LRVFNTSEDL
2060 2070 2080 2090 2100
SRVNATVQET NDLLHNSTMT TLLAGRKMKD MEMQANLLLD RLKPLKTLEE
2110 2120 2130 2140 2150
NLSRNLSEIK LLISRARKQV ASIKVAVSAD RDCIRAYQPQ TSSTNYNTLI
2160 2170 2180 2190 2200
LNVKTQEPDN LLFYLGSSSS SDFLAVEMRR GKVAFLWDLG SGSTRLEFPE
2210 2220 2230 2240 2250
VSINNNRWHS IYITRFGNMG SLSVKEASAA ENPPVRTSKS PGPSKVLDIN
2260 2270 2280 2290 2300
NSTLMFVGGL GGQIKKSPAV KVTHFKGCMG EAFLNGKSIG LWNYIEREGK
2310 2320 2330 2340 2350
CNGCFGSSQN EDSSFHFDGS GYAMVEKTLR PTVTQIVILF STFSPNGLLF
2360 2370 2380 2390 2400
YLASNGTKDF LSIELVRGRV KVMVDLGSGP LTLMTDRRYN NGTWYKIAFQ
2410 2420 2430 2440 2450
RNRKQGLLAV FDAYDTSDKE TKQGETPGAA SDLNRLEKDL IYVGGLPHSK
2460 2470 2480 2490 2500
AVRKGVSSRS YVGCIKNLEI SRSTFDLLRN SYGVRKGCAL EPIQSVSFLR
2510 2520 2530 2540 2550
GGYVEMPPKS LSPESSLLAT FATKNSSGIL LVALGKDAEE AGGAQAHVPF
2560 2570 2580 2590 2600
FSIMLLEGRI EVHVNSGDGT SLRKALLHAP TGSYSDGQEH SISLVRNRRV
2610 2620 2630 2640 2650
ITIQVDENSP VEMKLGPLTE GKTIDISNLY IGGLPEDKAT PMLKMRTSFH
2660 2670 2680 2690 2700
GCIKNVVLDA QLLDFTHATG SEQVELDTCL LAEEPMQSLH REHGELPPEP
2710 2720 2730 2740 2750
PTLPQPELCA VDTAPGYVAG AHQFGLSQNS HLVLPLNQSD VRKRLQVQLS
2760 2770 2780 2790 2800
IRTFASSGLI YYVAHQNQMD YATLQLQEGR LHFMFDLGKG RTKVSHPALL
2810 2820 2830 2840 2850
SDGKWHTVKT EYIKRKAFMT VDGQESPSVT VVGNATTLDV ERKLYLGGLP
2860 2870 2880 2890 2900
SHYRARNIGT ITHSIPACIG EIMVNGQQLD KDRPLSASAV DRCYVVAQEG
2910 2920 2930 2940 2950
TFFEGSGYAA LVKEGYKVRL DLNITLEFRT TSKNGVLLGI SSAKVDAIGL
2960 2970 2980 2990 3000
EIVDGKVLFH VNNGAGRITA TYQPRAARAL CDGKWHTLQA HKSKHRIVLT
3010 3020 3030 3040 3050
VDGNSVRAES PHTHSTSADT NDPIYVGGYP AHIKQNCLSS RASFRGCVRN
3060 3070 3080
LRLSRGSQVQ SLDLSRAFDL QGVFPHSCPG PEP
Length:3,083
Mass (Da):338,148
Last modified:July 18, 2018 - v2
Checksum:i4A7C156E40D85DC7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti209I → T in CAA30561 (PubMed:3267223).Curated1
Sequence conflicti656D → N in AAA39410 (PubMed:3182802).Curated1
Sequence conflicti920I → V in AAA39410 (PubMed:3182802).Curated1
Sequence conflicti1122G → S in AAA39410 (PubMed:3182802).Curated1
Sequence conflicti1131A → V in AAA39410 (PubMed:3182802).Curated1
Sequence conflicti1295R → Q in AAA39410 (PubMed:3182802).Curated1
Sequence conflicti1797K → KE in AAA39410 (PubMed:3182802).Curated1
Sequence conflicti1964S → G in AAA39410 (PubMed:3182802).Curated1
Sequence conflicti1990 – 1994MDNIM → VDNIT in AAA39410 (PubMed:3182802).Curated5
Sequence conflicti2120V → A in AAA39410 (PubMed:3182802).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04064 mRNA Translation: AAA39410.1
AC154823 Genomic DNA No translation available.
X07737 mRNA Translation: CAA30561.1
X13459 mRNA Translation: CAA31807.1
M36775 mRNA Translation: AAA39406.1
CCDSiCCDS37681.1
PIRiA31771 MMMSA
RefSeqiNP_032506.2, NM_008480.2
UniGeneiMm.303386

Genome annotation databases

EnsembliENSMUST00000035471; ENSMUSP00000043957; ENSMUSG00000032796
GeneIDi16772
KEGGimmu:16772

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04064 mRNA Translation: AAA39410.1
AC154823 Genomic DNA No translation available.
X07737 mRNA Translation: CAA30561.1
X13459 mRNA Translation: CAA31807.1
M36775 mRNA Translation: AAA39406.1
CCDSiCCDS37681.1
PIRiA31771 MMMSA
RefSeqiNP_032506.2, NM_008480.2
UniGeneiMm.303386

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JD4X-ray1.90A/B2705-3083[»]
5MC9X-ray2.13A2078-2706[»]
ProteinModelPortaliP19137
SMRiP19137
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201096, 8 interactors
ComplexPortaliCPX-3008 Laminin-111 complex
CPX-3010 Laminin-121 complex
IntActiP19137, 5 interactors
MINTiP19137
STRINGi10090.ENSMUSP00000043957

PTM databases

iPTMnetiP19137
PhosphoSitePlusiP19137

Proteomic databases

MaxQBiP19137
PaxDbiP19137
PeptideAtlasiP19137
PRIDEiP19137

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035471; ENSMUSP00000043957; ENSMUSG00000032796
GeneIDi16772
KEGGimmu:16772

Organism-specific databases

CTDi284217
MGIiMGI:99892 Lama1

Phylogenomic databases

eggNOGiKOG1836 Eukaryota
ENOG410XRDC LUCA
GeneTreeiENSGT00780000121851
HOGENOMiHOG000293201
HOVERGENiHBG052298
InParanoidiP19137
KOiK05637
OMAiICQPCEC
OrthoDBiEOG091G005L
PhylomeDBiP19137
TreeFamiTF335359

Enzyme and pathway databases

ReactomeiR-MMU-3000157 Laminin interactions
R-MMU-8874081 MET activates PTK2 signaling

Miscellaneous databases

EvolutionaryTraceiP19137
PROiPR:P19137
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032796 Expressed in 228 organ(s), highest expression level in maturing glomerular tuft (mouse)
CleanExiMM_LAMA1
GenevisibleiF8VQ40 MM

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR009254 Laminin_aI
IPR010307 Laminin_dom_II
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000034 Laminin_IV
IPR008211 Laminin_N
IPR038684 Laminin_N_sf
PfamiView protein in Pfam
PF00052 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
SMARTiView protein in SMART
SM00181 EGF, 10 hits
SM00180 EGF_Lam, 16 hits
SM00281 LamB, 2 hits
SM00282 LamG, 5 hits
SM00136 LamNT, 1 hit
SUPFAMiSSF49899 SSF49899, 5 hits
PROSITEiView protein in PROSITE
PS00022 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
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA1_MOUSE
AccessioniPrimary (citable) accession number: P19137
Secondary accession number(s): F8VQ40
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 18, 2018
Last modified: October 10, 2018
This is version 187 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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