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P19137

- LAMA1_MOUSE

UniProt

P19137 - LAMA1_MOUSE

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Protein
Laminin subunit alpha-1
Gene
Lama1, Lama, Lama-1
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
  3. protein binding Source: IntAct

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 complex Source: MGI
  7. laminin-1 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 Publication
Add
BLAST
Chaini25 – 30843060Laminin subunit alpha-1
PRO_0000017055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyrrolidone carboxylic acid
Glycosylationi45 – 451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi79 – 791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi277 ↔ 286 By similarity
Disulfide bondi279 ↔ 297 By similarity
Disulfide bondi299 ↔ 308 By similarity
Disulfide bondi311 ↔ 331 By similarity
Disulfide bondi334 ↔ 343 By similarity
Disulfide bondi336 ↔ 368 By similarity
Glycosylationi370 – 3701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi371 ↔ 380 By similarity
Glycosylationi374 – 3741N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi383 ↔ 401 By similarity
Disulfide bondi404 ↔ 416 By similarity
Disulfide bondi406 ↔ 434 By similarity
Disulfide bondi436 ↔ 445 By similarity
Disulfide bondi448 ↔ 458 By similarity
Disulfide bondi461 ↔ 474 By similarity
Disulfide bondi463 ↔ 478 By similarity
Disulfide bondi480 ↔ 489 By similarity
Disulfide bondi492 ↔ 507 By similarity
Glycosylationi531 – 5311N-linked (GlcNAc...) Reviewed prediction
Glycosylationi562 – 5621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi672 – 6721N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi749 ↔ 758 By similarity
Disulfide bondi751 ↔ 764 By similarity
Disulfide bondi767 ↔ 776 By similarity
Glycosylationi770 – 7701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi779 ↔ 795 By similarity
Disulfide bondi798 ↔ 813 By similarity
Disulfide bondi800 ↔ 823 By similarity
Disulfide bondi826 ↔ 835 By similarity
Disulfide bondi838 ↔ 853 By similarity
Disulfide bondi856 ↔ 870 By similarity
Glycosylationi857 – 8571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi858 ↔ 877 By similarity
Disulfide bondi880 ↔ 889 By similarity
Disulfide bondi892 ↔ 906 By similarity
Disulfide bondi909 ↔ 921 By similarity
Disulfide bondi911 ↔ 928 By similarity
Glycosylationi914 – 9141N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi930 ↔ 939 By similarity
Disulfide bondi942 ↔ 955 By similarity
Disulfide bondi958 ↔ 970 By similarity
Glycosylationi959 – 9591N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi960 ↔ 976 By similarity
Glycosylationi969 – 9691N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi978 ↔ 987 By similarity
Disulfide bondi990 ↔ 1002 By similarity
Disulfide bondi1005 ↔ 1014 By similarity
Disulfide bondi1007 ↔ 1021 By similarity
Disulfide bondi1023 ↔ 1032 By similarity
Disulfide bondi1035 ↔ 1048 By similarity
Disulfide bondi1051 ↔ 1063 By similarity
Glycosylationi1052 – 10521N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1053 ↔ 1070 By similarity
Disulfide bondi1072 ↔ 1081 By similarity
Disulfide bondi1084 ↔ 1094 By similarity
Disulfide bondi1097 ↔ 1109 By similarity
Disulfide bondi1099 ↔ 1125 By similarity
Disulfide bondi1127 ↔ 1136 By similarity
Disulfide bondi1139 ↔ 1154 By similarity
Glycosylationi1344 – 13441N-linked (GlcNAc...)1 Publication
Disulfide bondi1410 ↔ 1419 By similarity
Disulfide bondi1412 ↔ 1426 By similarity
Glycosylationi1414 – 14141N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1429 ↔ 1438 By similarity
Disulfide bondi1441 ↔ 1456 By similarity
Disulfide bondi1459 ↔ 1473 By similarity
Disulfide bondi1461 ↔ 1483 By similarity
Disulfide bondi1486 ↔ 1495 By similarity
Disulfide bondi1498 ↔ 1513 By similarity
Disulfide bondi1516 ↔ 1528 By similarity
Disulfide bondi1518 ↔ 1535 By similarity
Disulfide bondi1537 ↔ 1546 By similarity
Disulfide bondi1549 ↔ 1560 By similarity
Disulfide bondi1563 – 1563Interchain Inferred
Disulfide bondi1567 – 1567Interchain Inferred
Glycosylationi1586 – 15861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1603 – 16031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1659 – 16591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1686 – 16861N-linked (GlcNAc...)1 Publication
Glycosylationi1706 – 17061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1718 – 17181N-linked (GlcNAc...)1 Publication
Glycosylationi1725 – 17251N-linked (GlcNAc...)1 Publication
Glycosylationi1763 – 17631N-linked (GlcNAc...)1 Publication
Glycosylationi1812 – 18121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1902 – 19021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1906 – 19061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1936 – 19361N-linked (GlcNAc...)1 Publication
Glycosylationi1982 – 19821N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1993 – 19931N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1999 – 19991N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2027 – 20271N-linked (GlcNAc...)1 Publication
Glycosylationi2046 – 20461N-linked (GlcNAc...)1 Publication
Glycosylationi2055 – 20551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2062 – 20621N-linked (GlcNAc...); atypical1 Publication
Glycosylationi2067 – 20671N-linked (GlcNAc...)1 Publication
Glycosylationi2102 – 21021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2106 – 21061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2251 – 22511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2252 – 22521N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2279 ↔ 2305 By similarity
Glycosylationi2356 – 23561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2392 – 23921N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2465 ↔ 2489 By similarity
Glycosylationi2526 – 25261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2653 ↔ 2680 By similarity
Glycosylationi2738 – 27381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2835 – 28351N-linked (GlcNAc...)1 Publication
Disulfide bondi2869 ↔ 2894 By similarity
Glycosylationi2924 – 29241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3048 ↔ 3079 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, 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

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.

Miscellaneous databases

EvolutionaryTraceiP19137.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1612 – 1820209 Reviewed prediction
Add
BLAST
Coiled coili1869 – 190335 Reviewed prediction
Add
BLAST
Coiled coili2096 – 212833 Reviewed prediction
Add
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

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.
InterProiIPR008985. 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]
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

« Hide

MRGSGTGAAL LVLLASVLWV TVRSQQRGLF PAILNLATNA HISANATCGE     50
KGPEMFCKLV EHVPGRPVRH AQCRVCDGNS TNPRERHPIS HAIDGTNNWW 100
QSPSIQNGRE YHWVTVTLDL RQVFQVAYII IKAANAPRPG NWILERSVDG 150
VKFKPWQYYA VSDTECLTRY KITPRRGPPT YRADNEVICT SYYSKLVPLE 200
HGEIHTSLIN GRPSADDPSP QLLEFTSARY IRLRLQRIRT LNADLMTLSH 250
RDLRDLDPIV TRRYYYSIKD ISVGGMCICY GHASSCPWDE EAKQLQCQCE 300
HNTCGESCDR CCPGYHQQPW RPGTISSGNE CEECNCHNKA KDCYYDSSVA 350
KERRSLNTAG QYSGGGVCVN CSQNTTGINC ETCIDQYYRP HKVSPYDDHP 400
CRPCNCDPVG SLSSVCIKDD RHADLANGKW PGQCPCRKGY AGDKCDRCQF 450
GYRGFPNCIP CDCRTVGSLN EDPCIEPCLC KKNVEGKNCD RCKPGFYNLK 500
ERNPEGCSEC FCFGVSGVCD SLTWSISQVT NMSGWLVTDL MSTNKIRSQQ 550
DVLGGHRQIS INNTAVMQRL TSTYYWAAPE AYLGNKLTAF GGFLKYTVSY 600
DIPVETVDSD LMSHADIIIK GNGLTISTRA EGLSLQPYEE YFNVVRLVPE 650
NFRDFNTRRE IDRDQLMTVL ANVTHLLIRA NYNSAKMALY RLDSVSLDIA 700
SPNAIDLAVA ADVEHCECPQ GYTGTSCEAC LPGYYRVDGI LFGGICQPCE 750
CHGHASECDI HGICSVCTHN TTGDHCEQCL PGFYGTPSRG TPGDCQPCAC 800
PLSIDSNNFS PTCHLTDGEE VVCDQCAPGY SGSWCERCAD GYYGNPTVPG 850
GTCVPCNCSG NVDPLEAGHC DSVTGECLKC LWNTDGAHCE RCADGFYGDA 900
VTAKNCRACD CHENGSLSGV CHLETGLCDC KPHVTGQQCD QCLSGYYGLD 950
TGLGCVPCNC SVEGSVSDNC TEEGQCHCGP GVSGKQCDRC SHGFYAFQDG 1000
GCTPCDCAHT QNNCDPASGE CLCPPHTQGL KCEECEEAYW GLDPEQGCQA 1050
CNCSAVGSTS AQCDVLSGHC PCKKGFGGQS CHQCSLGYRS FPDCVPCGCD 1100
LRGTLPDTCD LEQGLCSCSE DSGTCSCKEN VVGPQCSKCQ AGTFALRGDN 1150
PQGCSPCFCF GLSQLCSELE GYVRTLITLA SDQPLLHVVS QSNLKGTIEG 1200
VHFQPPDTLL DAEAVRQHIY AEPFYWRLPK QFQGDQLLAY GGKLQYSVAF 1250
YSTLGTGTSN YEPQVLIKGG RARKHVIYMD APAPENGVRQ DYEVQMKEEF 1300
WKYFNSVSEK HVTHSDFMSV LSNIDYILIK ASYGQGLQQS RIANISMEVG 1350
RKAVELPAEG EAALLLELCV CPPGTAGHSC QDCAPGYYRE KLPESGGRGP 1400
RPLLAPCVPC NCNNHSDVCD PETGKCLSCR DHTSGDHCEL CASGYYGKVT 1450
GLPGDCTPCT CPHHPPFSFS PTCVVEGDSD FRCNACLPGY EGQYCERCSA 1500
GYHGNPRAAG GSCQTCDCNP QGSVHSDCDR ASGQCVCKPG ATGLHCEKCL 1550
PRHILMESDC VSCDDDCVGP LLNDLDSVGD AVLSLNLTGV SPAPYGILEN 1600
LENTTKYFQR YLIKENAKKI RAEIQLEGIA EQTENLQKEL TRVLARHQKV 1650
NAEMERTSNG TQALATFIEQ LHANIKEITE KVATLNQTAR KDFQPPVSAL 1700
QSMHQNISSL LGLIKERNFT EMQQNATLEL KAAKDLLSRI QKRFQKPQEK 1750
LKALKEANSL LSNHSEKLQA AEELLKEAGS KTQESNLLLL LVKANLKEEF 1800
QEKKLRVQEE QNVTSELIAK GREWVDAAGT HTAAAQDTLT QLEHHRDELL 1850
LWARKIRSHV DDLVMQMSKR RARDLVHRAE QHASELQSRA GALDRDLENV 1900
RNVSLNATSA AHVHSNIQTL TEEAEMLAAD AHKTANKTDL ISESLASRGK 1950
AVLQRSSRFL KESVGTRRKQ QGITMKLDEL KNLTSQFQES VDNITKQAND 2000
SLAMLRESPG GMREKGRKAR ELAAAANESA VKTLEDVLAL SLRVFNTSED 2050
LSRVNATVQE TNDLLHNSTM TTLLAGRKMK DMEMQANLLL DRLKPLKTLE 2100
ENLSRNLSEI KLLISRARKQ AASIKVAVSA DRDCIRAYQP QTSSTNYNTL 2150
ILNVKTQEPD NLLFYLGSSS SSDFLAVEMR RGKVAFLWDL GSGSTRLEFP 2200
EVSINNNRWH SIYITRFGNM GSLSVKEASA AENPPVRTSK SPGPSKVLDI 2250
NNSTLMFVGG LGGQIKKSPA VKVTHFKGCM GEAFLNGKSI GLWNYIEREG 2300
KCNGCFGSSQ NEDSSFHFDG SGYAMVEKTL RPTVTQIVIL FSTFSPNGLL 2350
FYLASNGTKD FLSIELVRGR VKVMVDLGSG PLTLMTDRRY NNGTWYKIAF 2400
QRNRKQGLLA VFDAYDTSDK ETKQGETPGA ASDLNRLEKD LIYVGGLPHS 2450
KAVRKGVSSR SYVGCIKNLE ISRSTFDLLR NSYGVRKGCA LEPIQSVSFL 2500
RGGYVEMPPK SLSPESSLLA TFATKNSSGI LLVALGKDAE EAGGAQAHVP 2550
FFSIMLLEGR IEVHVNSGDG TSLRKALLHA PTGSYSDGQE HSISLVRNRR 2600
VITIQVDENS PVEMKLGPLT EGKTIDISNL YIGGLPEDKA TPMLKMRTSF 2650
HGCIKNVVLD AQLLDFTHAT GSEQVELDTC LLAEEPMQSL HREHGELPPE 2700
PPTLPQPELC AVDTAPGYVA GAHQFGLSQN SHLVLPLNQS DVRKRLQVQL 2750
SIRTFASSGL IYYVAHQNQM DYATLQLQEG RLHFMFDLGK GRTKVSHPAL 2800
LSDGKWHTVK TEYIKRKAFM TVDGQESPSV TVVGNATTLD VERKLYLGGL 2850
PSHYRARNIG TITHSIPACI GEIMVNGQQL DKDRPLSASA VDRCYVVAQE 2900
GTFFEGSGYA ALVKEGYKVR LDLNITLEFR TTSKNGVLLG ISSAKVDAIG 2950
LEIVDGKVLF HVNNGAGRIT ATYQPRAARA LCDGKWHTLQ AHKSKHRIVL 3000
TVDGNSVRAE SPHTHSTSAD TNDPIYVGGY PAHIKQNCLS SRASFRGCVR 3050
NLRLSRGSQV QSLDLSRAFD LQGVFPHSCP GPEP 3084
Length:3,084
Mass (Da):338,172
Last modified:November 1, 1990 - v1
Checksum:iCF8E0D508046FC23
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091I → T1 Publication

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 IPR008985. 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 ]
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: September 3, 2014
This is version 152 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

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