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P19137

- LAMA1_MOUSE

UniProt

P19137 - LAMA1_MOUSE

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Protein

Laminin subunit alpha-1

Gene

Lama1

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.

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: MGI
  2. glycosphingolipid binding Source: MGI

GO - Biological processi

  1. branching involved in salivary gland morphogenesis Source: MGI
  2. cell adhesion Source: UniProtKB-KW
  3. cell surface receptor signaling pathway Source: MGI
  4. epithelial tube branching involved in lung morphogenesis Source: MGI
  5. establishment of epithelial cell apical/basal polarity Source: MGI
  6. morphogenesis of an epithelial sheet Source: MGI
  7. neuron projection development Source: MGI
  8. regulation of cell adhesion Source: InterPro
  9. regulation of cell migration Source: InterPro
  10. regulation of embryonic development Source: InterPro
  11. retina development in camera-type eye Source: MGI
  12. retinal blood vessel morphogenesis Source: MGI
  13. tissue development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_219680. 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
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:99892. Lama1.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: UniProtKB
  3. cell-cell junction Source: MGI
  4. extracellular matrix Source: MGI
  5. extracellular region Source: Reactome
  6. laminin-1 complex Source: MGI
  7. laminin complex Source: MGI
  8. proteinaceous extracellular matrix 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 – 24241 PublicationAdd
BLAST
Chaini25 – 30843060Laminin subunit alpha-1PRO_0000017055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyrrolidone carboxylic acid1 Publication
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi277 ↔ 286By similarity
Disulfide bondi279 ↔ 297By similarity
Disulfide bondi299 ↔ 308By similarity
Disulfide bondi311 ↔ 331By similarity
Disulfide bondi334 ↔ 343By similarity
Disulfide bondi336 ↔ 368By similarity
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi371 ↔ 380By similarity
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi562 – 5621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi672 – 6721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi749 ↔ 758By similarity
Disulfide bondi751 ↔ 764By similarity
Disulfide bondi767 ↔ 776By similarity
Glycosylationi770 – 7701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi779 ↔ 795By similarity
Disulfide bondi798 ↔ 813By similarity
Disulfide bondi800 ↔ 823By similarity
Disulfide bondi826 ↔ 835By similarity
Disulfide bondi838 ↔ 853By similarity
Disulfide bondi856 ↔ 870By similarity
Glycosylationi857 – 8571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi858 ↔ 877By similarity
Disulfide bondi880 ↔ 889By similarity
Disulfide bondi892 ↔ 906By similarity
Disulfide bondi909 ↔ 921By similarity
Disulfide bondi911 ↔ 928By similarity
Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi930 ↔ 939By similarity
Disulfide bondi942 ↔ 955By similarity
Disulfide bondi958 ↔ 970By similarity
Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi960 ↔ 976By similarity
Glycosylationi969 – 9691N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1052 – 10521N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1344 – 13441N-linked (GlcNAc...)1 Publication
Disulfide bondi1410 ↔ 1419By similarity
Disulfide bondi1412 ↔ 1426By similarity
Glycosylationi1414 – 14141N-linked (GlcNAc...)Sequence Analysis
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 bondi1563 – 1563InterchainCurated
Disulfide bondi1567 – 1567InterchainCurated
Glycosylationi1586 – 15861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1603 – 16031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1659 – 16591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1686 – 16861N-linked (GlcNAc...)1 Publication
Glycosylationi1706 – 17061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1718 – 17181N-linked (GlcNAc...)1 Publication
Glycosylationi1725 – 17251N-linked (GlcNAc...)1 Publication
Glycosylationi1763 – 17631N-linked (GlcNAc...)1 Publication
Glycosylationi1812 – 18121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1902 – 19021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1906 – 19061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1936 – 19361N-linked (GlcNAc...)1 Publication
Glycosylationi1982 – 19821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1993 – 19931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1999 – 19991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2027 – 20271N-linked (GlcNAc...)1 Publication
Glycosylationi2046 – 20461N-linked (GlcNAc...)1 Publication
Glycosylationi2055 – 20551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2062 – 20621N-linked (GlcNAc...); atypical1 Publication
Glycosylationi2067 – 20671N-linked (GlcNAc...)1 Publication
Glycosylationi2102 – 21021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2106 – 21061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2251 – 22511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2252 – 22521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2279 ↔ 2305By similarity
Glycosylationi2356 – 23561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2392 – 23921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2465 ↔ 2489By similarity
Glycosylationi2526 – 25261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2653 ↔ 2680By similarity
Glycosylationi2738 – 27381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2835 – 28351N-linked (GlcNAc...)1 Publication
Disulfide bondi2869 ↔ 2894By similarity
Glycosylationi2924 – 29241N-linked (GlcNAc...)Sequence Analysis
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.
PRIDEiP19137.

PTM databases

PhosphoSiteiP19137.

Expressioni

Gene expression databases

CleanExiMM_LAMA1.
GenevestigatoriP19137.

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 interactions.
IntActiP19137. 4 interactions.
MINTiMINT-2635122.
STRINGi10090.ENSMUSP00000043957.

Structurei

Secondary structure

1
3084
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2732 – 27365
Beta strandi2743 – 275412
Beta strandi2759 – 27657
Beta strandi2769 – 277810
Beta strandi2781 – 27877
Beta strandi2792 – 27965
Beta strandi2803 – 28053
Beta strandi2807 – 28148
Beta strandi2817 – 28226
Beta strandi2843 – 28497
Beta strandi2868 – 28758
Beta strandi2886 – 28905
Beta strandi2895 – 291723
Beta strandi2923 – 293210
Beta strandi2936 – 29427
Beta strandi2944 – 29463
Beta strandi2948 – 29547
Beta strandi2957 – 296610
Beta strandi2968 – 29736
Helixi2980 – 29823
Beta strandi2983 – 29853
Beta strandi2987 – 29948
Beta strandi2997 – 30026
Beta strandi3005 – 30095
Beta strandi3023 – 30286
Beta strandi3046 – 30549
Helixi3065 – 30673
Beta strandi3069 – 30757
Beta strandi3079 – 30813

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JD4X-ray1.90A/B2706-3084[»]
ProteinModelPortaliP19137.
SMRiP19137. Positions 29-523, 715-1154, 1369-1558, 2140-3083.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19137.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 276252Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini277 – 33357Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini334 – 40370Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini404 – 46057Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini461 – 50949Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini510 – 51910Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini523 – 715193Laminin IV type A 1PROSITE-ProRule annotationAdd
BLAST
Domaini716 – 74833Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini749 – 79749Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini798 – 85558Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini856 – 90853Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini909 – 95749Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini958 – 100447Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1005 – 105046Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1051 – 109646Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1097 – 115660Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1157 – 116610Laminin EGF-like 14; first partPROSITE-ProRule annotation
Domaini1177 – 1368192Laminin IV type A 2PROSITE-ProRule annotationAdd
BLAST
Domaini1369 – 140941Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1410 – 145849Laminin EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini1459 – 151557Laminin EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini1516 – 156247Laminin EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini2125 – 2305181Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2313 – 2489177Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini2494 – 2680187Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini2722 – 2894173Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini2899 – 3079181Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1564 – 2124561Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1612 – 1820209Sequence AnalysisAdd
BLAST
Coiled coili1869 – 190335Sequence AnalysisAdd
BLAST
Coiled coili2096 – 212833Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1147 – 11493Cell attachment site

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

eggNOGiNOG247347.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiP19137.
KOiK05637.
PhylomeDBiP19137.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 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]
SMARTiSM00180. EGF_Lam. 15 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

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        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091I → T(PubMed:3267223)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
J04064 mRNA. Translation: AAA39410.1 .
X07737 mRNA. Translation: CAA30561.1 .
X13459 mRNA. Translation: CAA31807.1 .
M36775 mRNA. Translation: AAA39406.1 .
PIRi A31771. MMMSA.
RefSeqi NP_032506.2. NM_008480.2.
UniGenei Mm.303386.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JD4 X-ray 1.90 A/B 2706-3084 [» ]
ProteinModelPortali P19137.
SMRi P19137. Positions 29-523, 715-1154, 1369-1558, 2140-3083.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201096. 7 interactions.
IntActi P19137. 4 interactions.
MINTi MINT-2635122.
STRINGi 10090.ENSMUSP00000043957.

PTM databases

PhosphoSitei P19137.

Proteomic databases

MaxQBi P19137.
PaxDbi P19137.
PRIDEi P19137.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 16772.
KEGGi mmu:16772.

Organism-specific databases

CTDi 284217.
MGIi MGI:99892. Lama1.

Phylogenomic databases

eggNOGi NOG247347.
HOGENOMi HOG000293201.
HOVERGENi HBG052298.
InParanoidi P19137.
KOi K05637.
PhylomeDBi P19137.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_219680. L1CAM interactions.

Miscellaneous databases

EvolutionaryTracei P19137.
NextBioi 290602.
PROi P19137.
SOURCEi Search...

Gene expression databases

CleanExi MM_LAMA1.
Genevestigatori P19137.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. Laminin_B. 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 ]
SMARTi SM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 5 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

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: October 29, 2014
This is version 154 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

External Data

Dasty 3