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Protein

Laminin subunit alpha-1

Gene

Lama1

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

GO - Molecular functioni

  • extracellular matrix structural constituent Source: MGI
  • glycosphingolipid binding Source: MGI

GO - Biological processi

  • axon guidance Source: Reactome
  • branching involved in salivary gland morphogenesis Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • cell surface receptor signaling pathway Source: MGI
  • epithelial tube branching involved in lung morphogenesis Source: MGI
  • establishment of epithelial cell apical/basal polarity Source: MGI
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • morphogenesis of an epithelial sheet Source: MGI
  • neuron projection development Source: MGI
  • protein phosphorylation Source: CACAO
  • regulation of cell adhesion Source: InterPro
  • regulation of cell migration Source: InterPro
  • regulation of embryonic development Source: InterPro
  • retina development in camera-type eye Source: MGI
  • retinal blood vessel morphogenesis Source: MGI
  • tissue development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-373760. L1CAM interactions.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:99892. Lama1.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: MGI
  • basement membrane Source: UniProtKB
  • cell-cell junction Source: MGI
  • extracellular matrix Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
  • laminin-1 complex Source: MGI
  • laminin-3 complex Source: MGI
  • laminin complex Source: MGI
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001705525 – 3084Laminin subunit alpha-1Add BLAST3060

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Pyrrolidone carboxylic acid1 Publication1
Glycosylationi45N-linked (GlcNAc...)Sequence analysis1
Glycosylationi79N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi277 ↔ 286By similarity
Disulfide bondi279 ↔ 297By similarity
Disulfide bondi299 ↔ 308By similarity
Disulfide bondi311 ↔ 331By similarity
Disulfide bondi334 ↔ 343By similarity
Disulfide bondi336 ↔ 368By similarity
Glycosylationi370N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi371 ↔ 380By similarity
Glycosylationi374N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi383 ↔ 401By similarity
Disulfide bondi404 ↔ 416By similarity
Disulfide bondi406 ↔ 434By similarity
Disulfide bondi436 ↔ 445By similarity
Disulfide bondi448 ↔ 458By similarity
Disulfide bondi461 ↔ 474By similarity
Disulfide bondi463 ↔ 478By similarity
Disulfide bondi480 ↔ 489By similarity
Disulfide bondi492 ↔ 507By similarity
Glycosylationi531N-linked (GlcNAc...)Sequence analysis1
Glycosylationi562N-linked (GlcNAc...)Sequence analysis1
Glycosylationi672N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi749 ↔ 758By similarity
Disulfide bondi751 ↔ 764By similarity
Disulfide bondi767 ↔ 776By similarity
Glycosylationi770N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi779 ↔ 795By similarity
Disulfide bondi798 ↔ 813By similarity
Disulfide bondi800 ↔ 823By similarity
Disulfide bondi826 ↔ 835By similarity
Disulfide bondi838 ↔ 853By similarity
Disulfide bondi856 ↔ 870By similarity
Glycosylationi857N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi858 ↔ 877By similarity
Disulfide bondi880 ↔ 889By similarity
Disulfide bondi892 ↔ 906By similarity
Disulfide bondi909 ↔ 921By similarity
Disulfide bondi911 ↔ 928By similarity
Glycosylationi914N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi930 ↔ 939By similarity
Disulfide bondi942 ↔ 955By similarity
Disulfide bondi958 ↔ 970By similarity
Glycosylationi959N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi960 ↔ 976By similarity
Glycosylationi969N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi978 ↔ 987By similarity
Disulfide bondi990 ↔ 1002By similarity
Disulfide bondi1005 ↔ 1014By similarity
Disulfide bondi1007 ↔ 1021By similarity
Disulfide bondi1023 ↔ 1032By similarity
Disulfide bondi1035 ↔ 1048By similarity
Disulfide bondi1051 ↔ 1063By similarity
Glycosylationi1052N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1053 ↔ 1070By similarity
Disulfide bondi1072 ↔ 1081By similarity
Disulfide bondi1084 ↔ 1094By similarity
Disulfide bondi1097 ↔ 1109By similarity
Disulfide bondi1099 ↔ 1125By similarity
Disulfide bondi1127 ↔ 1136By similarity
Disulfide bondi1139 ↔ 1154By similarity
Glycosylationi1344N-linked (GlcNAc...)1 Publication1
Disulfide bondi1410 ↔ 1419By similarity
Disulfide bondi1412 ↔ 1426By similarity
Glycosylationi1414N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1429 ↔ 1438By similarity
Disulfide bondi1441 ↔ 1456By similarity
Disulfide bondi1459 ↔ 1473By similarity
Disulfide bondi1461 ↔ 1483By similarity
Disulfide bondi1486 ↔ 1495By similarity
Disulfide bondi1498 ↔ 1513By similarity
Disulfide bondi1516 ↔ 1528By similarity
Disulfide bondi1518 ↔ 1535By similarity
Disulfide bondi1537 ↔ 1546By similarity
Disulfide bondi1549 ↔ 1560By similarity
Disulfide bondi1563InterchainCurated
Disulfide bondi1567InterchainCurated
Glycosylationi1586N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1603N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1659N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1686N-linked (GlcNAc...)1 Publication1
Glycosylationi1706N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1718N-linked (GlcNAc...)1 Publication1
Glycosylationi1725N-linked (GlcNAc...)1 Publication1
Glycosylationi1763N-linked (GlcNAc...)1 Publication1
Glycosylationi1812N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1902N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1906N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1936N-linked (GlcNAc...)1 Publication1
Glycosylationi1982N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1993N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1999N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2027N-linked (GlcNAc...)1 Publication1
Glycosylationi2046N-linked (GlcNAc...)1 Publication1
Glycosylationi2055N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2062N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi2067N-linked (GlcNAc...)1 Publication1
Glycosylationi2102N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2106N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2251N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2252N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2279 ↔ 2305By similarity
Glycosylationi2356N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2392N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2465 ↔ 2489By similarity
Glycosylationi2526N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2653 ↔ 2680By similarity
Glycosylationi2738N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2835N-linked (GlcNAc...)1 Publication1
Disulfide bondi2869 ↔ 2894By similarity
Glycosylationi2924N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3048 ↔ 3079By similarity

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

CleanExiMM_LAMA1.

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 a different organism.

Protein-protein interaction databases

BioGridi201096. 7 interactors.
IntActiP19137. 5 interactors.
MINTiMINT-2635122.
STRINGi10090.ENSMUSP00000043957.

Structurei

Secondary structure

13084
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2732 – 2736Combined sources5
Beta strandi2743 – 2754Combined sources12
Beta strandi2759 – 2765Combined sources7
Beta strandi2769 – 2778Combined sources10
Beta strandi2781 – 2787Combined sources7
Beta strandi2792 – 2796Combined sources5
Beta strandi2803 – 2805Combined sources3
Beta strandi2807 – 2814Combined sources8
Beta strandi2817 – 2822Combined sources6
Beta strandi2843 – 2849Combined sources7
Beta strandi2868 – 2875Combined sources8
Beta strandi2886 – 2890Combined sources5
Beta strandi2895 – 2917Combined sources23
Beta strandi2923 – 2932Combined sources10
Beta strandi2936 – 2942Combined sources7
Beta strandi2944 – 2946Combined sources3
Beta strandi2948 – 2954Combined sources7
Beta strandi2957 – 2966Combined sources10
Beta strandi2968 – 2973Combined sources6
Helixi2980 – 2982Combined sources3
Beta strandi2983 – 2985Combined sources3
Beta strandi2987 – 2994Combined sources8
Beta strandi2997 – 3002Combined sources6
Beta strandi3005 – 3009Combined sources5
Beta strandi3023 – 3028Combined sources6
Beta strandi3046 – 3054Combined sources9
Helixi3065 – 3067Combined sources3
Beta strandi3069 – 3075Combined sources7
Beta strandi3079 – 3081Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JD4X-ray1.90A/B2706-3084[»]
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
Domaini2125 – 2305Laminin G-like 1PROSITE-ProRule annotationAdd BLAST181
Domaini2313 – 2489Laminin G-like 2PROSITE-ProRule annotationAdd BLAST177
Domaini2494 – 2680Laminin G-like 3PROSITE-ProRule annotationAdd BLAST187
Domaini2722 – 2894Laminin G-like 4PROSITE-ProRule annotationAdd BLAST173
Domaini2899 – 3079Laminin G-like 5PROSITE-ProRule annotationAdd BLAST181

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1564 – 2124Domain II and IAdd BLAST561

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1612 – 1820Sequence analysisAdd BLAST209
Coiled coili1869 – 1903Sequence analysisAdd BLAST35
Coiled coili2096 – 2128Sequence analysisAdd BLAST33

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.

Sequence similaritiesi

Contains 17 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation
Contains 2 laminin IV type A domains.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiP19137.
KOiK05637.
PhylomeDBiP19137.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. 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]
SMARTiSM00181. EGF. 10 hits.
SM00180. EGF_Lam. 16 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. 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]

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
NFRDFNTRRE 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 CHENGSLSGV 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 DSGTCSCKEN VVGPQCSKCQ 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 DYEVQMKEEF
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 LVKANLKEEF
1810 1820 1830 1840 1850
QEKKLRVQEE QNVTSELIAK GREWVDAAGT HTAAAQDTLT QLEHHRDELL
1860 1870 1880 1890 1900
LWARKIRSHV DDLVMQMSKR RARDLVHRAE QHASELQSRA GALDRDLENV
1910 1920 1930 1940 1950
RNVSLNATSA AHVHSNIQTL TEEAEMLAAD AHKTANKTDL ISESLASRGK
1960 1970 1980 1990 2000
AVLQRSSRFL KESVGTRRKQ QGITMKLDEL KNLTSQFQES VDNITKQAND
2010 2020 2030 2040 2050
SLAMLRESPG GMREKGRKAR ELAAAANESA VKTLEDVLAL SLRVFNTSED
2060 2070 2080 2090 2100
LSRVNATVQE TNDLLHNSTM TTLLAGRKMK DMEMQANLLL DRLKPLKTLE
2110 2120 2130 2140 2150
ENLSRNLSEI KLLISRARKQ AASIKVAVSA DRDCIRAYQP QTSSTNYNTL
2160 2170 2180 2190 2200
ILNVKTQEPD NLLFYLGSSS SSDFLAVEMR RGKVAFLWDL GSGSTRLEFP
2210 2220 2230 2240 2250
EVSINNNRWH SIYITRFGNM GSLSVKEASA AENPPVRTSK SPGPSKVLDI
2260 2270 2280 2290 2300
NNSTLMFVGG LGGQIKKSPA VKVTHFKGCM GEAFLNGKSI GLWNYIEREG
2310 2320 2330 2340 2350
KCNGCFGSSQ NEDSSFHFDG SGYAMVEKTL RPTVTQIVIL FSTFSPNGLL
2360 2370 2380 2390 2400
FYLASNGTKD FLSIELVRGR VKVMVDLGSG PLTLMTDRRY NNGTWYKIAF
2410 2420 2430 2440 2450
QRNRKQGLLA VFDAYDTSDK ETKQGETPGA ASDLNRLEKD LIYVGGLPHS
2460 2470 2480 2490 2500
KAVRKGVSSR SYVGCIKNLE ISRSTFDLLR NSYGVRKGCA LEPIQSVSFL
2510 2520 2530 2540 2550
RGGYVEMPPK SLSPESSLLA TFATKNSSGI LLVALGKDAE EAGGAQAHVP
2560 2570 2580 2590 2600
FFSIMLLEGR IEVHVNSGDG TSLRKALLHA PTGSYSDGQE HSISLVRNRR
2610 2620 2630 2640 2650
VITIQVDENS PVEMKLGPLT EGKTIDISNL YIGGLPEDKA TPMLKMRTSF
2660 2670 2680 2690 2700
HGCIKNVVLD AQLLDFTHAT GSEQVELDTC LLAEEPMQSL HREHGELPPE
2710 2720 2730 2740 2750
PPTLPQPELC AVDTAPGYVA GAHQFGLSQN SHLVLPLNQS DVRKRLQVQL
2760 2770 2780 2790 2800
SIRTFASSGL IYYVAHQNQM DYATLQLQEG RLHFMFDLGK GRTKVSHPAL
2810 2820 2830 2840 2850
LSDGKWHTVK TEYIKRKAFM TVDGQESPSV TVVGNATTLD VERKLYLGGL
2860 2870 2880 2890 2900
PSHYRARNIG TITHSIPACI GEIMVNGQQL DKDRPLSASA VDRCYVVAQE
2910 2920 2930 2940 2950
GTFFEGSGYA ALVKEGYKVR LDLNITLEFR TTSKNGVLLG ISSAKVDAIG
2960 2970 2980 2990 3000
LEIVDGKVLF HVNNGAGRIT ATYQPRAARA LCDGKWHTLQ AHKSKHRIVL
3010 3020 3030 3040 3050
TVDGNSVRAE SPHTHSTSAD TNDPIYVGGY PAHIKQNCLS SRASFRGCVR
3060 3070 3080
NLRLSRGSQV QSLDLSRAFD LQGVFPHSCP GPEP
Length:3,084
Mass (Da):338,172
Last modified:November 1, 1990 - v1
Checksum:iCF8E0D508046FC23
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti209I → T (PubMed:3267223).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04064 mRNA. Translation: AAA39410.1.
X07737 mRNA. Translation: CAA30561.1.
X13459 mRNA. Translation: CAA31807.1.
M36775 mRNA. Translation: AAA39406.1.
PIRiA31771. MMMSA.
RefSeqiNP_032506.2. NM_008480.2.
UniGeneiMm.303386.

Genome annotation databases

GeneIDi16772.
KEGGimmu:16772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04064 mRNA. Translation: AAA39410.1.
X07737 mRNA. Translation: CAA30561.1.
X13459 mRNA. Translation: CAA31807.1.
M36775 mRNA. Translation: AAA39406.1.
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/B2706-3084[»]
ProteinModelPortaliP19137.
SMRiP19137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201096. 7 interactors.
IntActiP19137. 5 interactors.
MINTiMINT-2635122.
STRINGi10090.ENSMUSP00000043957.

PTM databases

iPTMnetiP19137.
PhosphoSitePlusiP19137.

Proteomic databases

MaxQBiP19137.
PaxDbiP19137.
PeptideAtlasiP19137.
PRIDEiP19137.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16772.
KEGGimmu:16772.

Organism-specific databases

CTDi284217.
MGIiMGI:99892. Lama1.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiP19137.
KOiK05637.
PhylomeDBiP19137.

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-373760. L1CAM interactions.

Miscellaneous databases

EvolutionaryTraceiP19137.
PROiP19137.
SOURCEiSearch...

Gene expression databases

CleanExiMM_LAMA1.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. 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]
SMARTiSM00181. EGF. 10 hits.
SM00180. EGF_Lam. 16 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA1_MOUSE
AccessioniPrimary (citable) accession number: P19137
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 171 of the entry and version 1 of the sequence. [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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.