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Protein

Laminin subunit beta-2

Gene

Lamb2

Organism
Rattus norvegicus (Rat)
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 - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-2
Alternative name(s):
Laminin chain B3
Laminin-11 subunit beta
Laminin-14 subunit beta
Laminin-15 subunit beta
Laminin-3 subunit beta
Laminin-4 subunit beta
Laminin-7 subunit beta
Laminin-9 subunit beta
S-laminin subunit beta
Short name:
S-LAM beta
Gene namesi
Name:Lamb2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2988. Lamb2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Add BLAST35
ChainiPRO_000001707036 – 1801Laminin subunit beta-2Add BLAST1766

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi251N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi286 ↔ 295PROSITE-ProRule annotation
Disulfide bondi288 ↔ 313PROSITE-ProRule annotation
Disulfide bondi315 ↔ 324PROSITE-ProRule annotation
Disulfide bondi327 ↔ 347PROSITE-ProRule annotation
Disulfide bondi350 ↔ 359PROSITE-ProRule annotation
Disulfide bondi352 ↔ 377PROSITE-ProRule annotation
Glycosylationi371N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi380 ↔ 389PROSITE-ProRule annotation
Disulfide bondi392 ↔ 410PROSITE-ProRule annotation
Disulfide bondi413 ↔ 426PROSITE-ProRule annotation
Disulfide bondi415 ↔ 441PROSITE-ProRule annotation
Disulfide bondi443 ↔ 452PROSITE-ProRule annotation
Disulfide bondi455 ↔ 470PROSITE-ProRule annotation
Disulfide bondi473 ↔ 487PROSITE-ProRule annotation
Disulfide bondi475 ↔ 494PROSITE-ProRule annotation
Disulfide bondi496 ↔ 505PROSITE-ProRule annotation
Disulfide bondi508 ↔ 522PROSITE-ProRule annotation
Disulfide bondi525 ↔ 537PROSITE-ProRule annotation
Disulfide bondi527 ↔ 544PROSITE-ProRule annotation
Disulfide bondi546 ↔ 555PROSITE-ProRule annotation
Disulfide bondi786 ↔ 798PROSITE-ProRule annotation
Disulfide bondi788 ↔ 805PROSITE-ProRule annotation
Disulfide bondi807 ↔ 816PROSITE-ProRule annotation
Disulfide bondi819 ↔ 831PROSITE-ProRule annotation
Disulfide bondi834 ↔ 846PROSITE-ProRule annotation
Disulfide bondi836 ↔ 853PROSITE-ProRule annotation
Disulfide bondi855 ↔ 864PROSITE-ProRule annotation
Disulfide bondi867 ↔ 877PROSITE-ProRule annotation
Disulfide bondi880 ↔ 889PROSITE-ProRule annotation
Disulfide bondi882 ↔ 896PROSITE-ProRule annotation
Disulfide bondi899 ↔ 908PROSITE-ProRule annotation
Disulfide bondi911 ↔ 927PROSITE-ProRule annotation
Disulfide bondi930 ↔ 946PROSITE-ProRule annotation
Disulfide bondi932 ↔ 957PROSITE-ProRule annotation
Disulfide bondi959 ↔ 968PROSITE-ProRule annotation
Disulfide bondi971 ↔ 986PROSITE-ProRule annotation
Disulfide bondi989 ↔ 1003PROSITE-ProRule annotation
Disulfide bondi991 ↔ 1010PROSITE-ProRule annotation
Disulfide bondi1013 ↔ 1022PROSITE-ProRule annotation
Disulfide bondi1025 ↔ 1038PROSITE-ProRule annotation
Disulfide bondi1041 ↔ 1061PROSITE-ProRule annotation
Disulfide bondi1043 ↔ 1068PROSITE-ProRule annotation
Disulfide bondi1070 ↔ 1079PROSITE-ProRule annotation
Disulfide bondi1082 ↔ 1095PROSITE-ProRule annotation
Glycosylationi1088N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1098 ↔ 1110PROSITE-ProRule annotation
Disulfide bondi1100 ↔ 1117PROSITE-ProRule annotation
Disulfide bondi1119 ↔ 1128PROSITE-ProRule annotation
Disulfide bondi1131 ↔ 1143PROSITE-ProRule annotation
Disulfide bondi1146 ↔ 1158PROSITE-ProRule annotation
Disulfide bondi1148 ↔ 1165PROSITE-ProRule annotation
Disulfide bondi1167 ↔ 1176PROSITE-ProRule annotation
Disulfide bondi1179 ↔ 1190PROSITE-ProRule annotation
Disulfide bondi1193InterchainCurated
Disulfide bondi1196InterchainCurated
Glycosylationi1252N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1311N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1351N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1502N-linked (GlcNAc...)Sequence analysis1
Modified residuei1535PhosphoserineBy similarity1
Disulfide bondi1800InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP15800.
PRIDEiP15800.

PTM databases

iPTMnetiP15800.
PhosphoSitePlusiP15800.
UniCarbKBiP15800.

Expressioni

Tissue specificityi

Found in the basement membranes (major component). S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.

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. Beta-2 is a subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9 (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and laminin-15 (laminin-523).

Protein-protein interaction databases

MINTiMINT-4655533.
STRINGi10116.ENSRNOP00000065052.

Structurei

Secondary structure

11801
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni529 – 531Combined sources3
Beta strandi532 – 536Combined sources5
Turni539 – 541Combined sources3
Beta strandi550 – 552Combined sources3
Beta strandi562 – 564Combined sources3
Beta strandi570 – 573Combined sources4
Helixi574 – 576Combined sources3
Beta strandi578 – 580Combined sources3
Beta strandi583 – 586Combined sources4
Beta strandi601 – 605Combined sources5
Beta strandi610 – 615Combined sources6
Beta strandi619 – 631Combined sources13
Beta strandi638 – 646Combined sources9
Turni656 – 659Combined sources4
Helixi662 – 665Combined sources4
Beta strandi666 – 671Combined sources6
Beta strandi676 – 679Combined sources4
Beta strandi684 – 686Combined sources3
Beta strandi692 – 702Combined sources11
Beta strandi716 – 725Combined sources10
Helixi727 – 729Combined sources3
Helixi731 – 734Combined sources4
Beta strandi735 – 737Combined sources3
Helixi738 – 749Combined sources12
Helixi752 – 756Combined sources5
Beta strandi757 – 759Combined sources3
Helixi768 – 780Combined sources13
Turni790 – 792Combined sources3
Turni813 – 816Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5LF2X-ray1.85A/B523-833[»]
ProteinModelPortaliP15800.
SMRiP15800.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 285Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini286 – 349Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST64
Domaini350 – 412Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST63
Domaini413 – 472Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST60
Domaini473 – 524Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST52
Domaini525 – 555Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd BLAST31
Domaini564 – 780Laminin IV type BPROSITE-ProRule annotationAdd BLAST217
Domaini786 – 833Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST48
Domaini834 – 879Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST46
Domaini880 – 929Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST50
Domaini930 – 988Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST59
Domaini989 – 1040Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST52
Domaini1041 – 1097Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST57
Domaini1098 – 1145Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST48
Domaini1146 – 1192Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1193 – 1412Domain IIAdd BLAST220
Regioni1413 – 1445Domain alphaAdd BLAST33
Regioni1446 – 1801Domain IAdd BLAST356

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1259 – 1306Sequence analysisAdd BLAST48
Coiled coili1475 – 1529Sequence analysisAdd BLAST55
Coiled coili1576 – 1793Sequence analysisAdd BLAST218

Domaini

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

Sequence similaritiesi

Contains 13 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type B domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
HOVERGENiHBG052301.
InParanoidiP15800.
KOiK06243.
PhylomeDBiP15800.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 10 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 10 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 12 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15800-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEWASGKPGR GRQGQPVPWE LRLGLLLSVL AATLAQVPSL DVPGCSRGSC
60 70 80 90 100
YPATGDLLVG RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRRPF
110 120 130 140 150
SARDNPNSHR IQNVVTSFAP QRRTAWWQSE NGVPMVTIQL DLEAEFHFTH
160 170 180 190 200
LIMTFKTFRP AAMLVERSAD FGRTWRVYRY FSYDCGADFP GIPLAPPRRW
210 220 230 240 250
DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ NLLKITNLRV
260 270 280 290 300
NLTRLHTLGD NLLDPRREIR EKYYYALYEL VIRGNCFCYG HASQCAPAPG
310 320 330 340 350
APAHAEGMVH GACICKHNTR GLNCEQCQDF YQDLPWHPAE DGHTHACRKC
360 370 380 390 400
ECNGHSHSCH FDMAVYLASG NVSGGVCDGC QHNTAGRHCE LCRPFFYRDP
410 420 430 440 450
TKDMRDPAAC RPCDCDPMGS QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGT
460 470 480 490 500
RCQQCRDGFF GLSASNPRGC QRCQCNSRGT VPGGTPCDSS SGTCFCKRLV
510 520 530 540 550
TGDGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA TGQCPCRPHM
560 570 580 590 600
IGRRCEQVQP GYFRPFLDHL TWEAEGAHGQ VLEVVERLVT NRETPSWTGV
610 620 630 640 650
GFVRLREGQE VEFLVTSLPR AMDYDLLLRW EPQVPEQWAE LELVVQRPGP
660 670 680 690 700
VSAHSPCGHV LPRDDRIQGM LHPNTRVLVF PRPVCLEPGL SYKLKLKLTG
710 720 730 740 750
TGGRAHPETP YSGSGILIDS LVLQPHVLML EMFSGGDAAA LERRTTFERY
760 770 780 790 800
RCHEEGLMPS KTPLSEACVP LLISASSLVY NGALPCQCDP QGSLSSECNP
810 820 830 840 850
HGGQCRCKPG VVGRRCDACA TGYYGFGPAG CQACQCSPDG ALSALCEGTS
860 870 880 890 900
GQCLCRTGAF GLRCDHCQRG QWGFPNCRPC VCNGRADECD AHTGACLGCR
910 920 930 940 950
DYTGGEHCER CIAGFHGDPR LPYGGQCRPC PCPEGPGSQR HFATSCHRDG
960 970 980 990 1000
YSQQIVCHCR AGYTGLRCEA CAPGHFGDPS KPGGRCQLCE CSGNIDPTDP
1010 1020 1030 1040 1050
GACDPHTGQC LRCLHHTEGP HCGHCKPGFH GQAARQSCHR CTCNLLGTDP
1060 1070 1080 1090 1100
QRCPSTDLCH CDPSTGQCPC LPHVQGLSCD RCAPNFWNFT SGRGCQPCAC
1110 1120 1130 1140 1150
HPSRARGPTC NEFTGQCHCH AGFGGRTCSE CQELHWGDPG LQCRACDCDP
1160 1170 1180 1190 1200
RGIDKPQCHR STGHCSCRPG VSGVRCDQCA RGFSGVFPAC HPCHACFGDW
1210 1220 1230 1240 1250
DRVVQDLAAR TRRLEQWAQE LQQTGVLGAF ESSFLNLQGK LGMVQAIVAA
1260 1270 1280 1290 1300
RNTSAASTAK LVEATEGLRH EIGKTTERLT QLEAELTDVQ DENFNANHAL
1310 1320 1330 1340 1350
SGLERDGLAL NLTLRQLDQH LDILKHSNFL GAYDSIRHAH SQSTEAERRA
1360 1370 1380 1390 1400
NASTFAIPSP VSNSADTRRR AEVLMGAQRE NFNRQHLANQ QALGRLSTHT
1410 1420 1430 1440 1450
HTLSLTGVNE LVCGAPGDAP CATSPCGGAG CRDEDGQPRC GGLGCSGAAA
1460 1470 1480 1490 1500
TADLALGRAR HTQAELQRAL VEGGGILSRV SETRRQAEEA QQRAQAALDK
1510 1520 1530 1540 1550
ANASRGQVEQ ANQELRELIQ NVKDFLSQEG ADPDSIEMVA TRVLDISIPA
1560 1570 1580 1590 1600
SPEQIQRLAS EIAERVRSLA DVDTILAHTM GDVRRAEQLL QDAQRARSRA
1610 1620 1630 1640 1650
EGERQKAETV QAALEEAQRA QGAAQGAIRG AVVDTKNTEQ TLQQVQERMA
1660 1670 1680 1690 1700
GTEQSLNSAS ERARQLHALL EALKLKRAGN SLAASTAEET AGSAQSRARE
1710 1720 1730 1740 1750
AEKQLREQVG DQYQTVRALA ERKAEGVLAA QARAEQLRDE ARGLLQAAQD
1760 1770 1780 1790 1800
KLQRLQELEG TYEENERELE VKAAQLDGLE ARMRSVLQAI NLQVQIYNTC

Q
Length:1,801
Mass (Da):196,474
Last modified:April 1, 1990 - v1
Checksum:i97AEF32F8F31FA75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16563 mRNA. Translation: CAA34561.1.
PIRiS03539. MMRTS.
RefSeqiNP_037106.1. NM_012974.1.
UniGeneiRn.774.

Genome annotation databases

GeneIDi25473.
KEGGirno:25473.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16563 mRNA. Translation: CAA34561.1.
PIRiS03539. MMRTS.
RefSeqiNP_037106.1. NM_012974.1.
UniGeneiRn.774.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5LF2X-ray1.85A/B523-833[»]
ProteinModelPortaliP15800.
SMRiP15800.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4655533.
STRINGi10116.ENSRNOP00000065052.

PTM databases

iPTMnetiP15800.
PhosphoSitePlusiP15800.
UniCarbKBiP15800.

Proteomic databases

PaxDbiP15800.
PRIDEiP15800.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25473.
KEGGirno:25473.

Organism-specific databases

CTDi3913.
RGDi2988. Lamb2.

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
HOVERGENiHBG052301.
InParanoidiP15800.
KOiK06243.
PhylomeDBiP15800.

Miscellaneous databases

PROiP15800.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 10 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 10 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 12 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMB2_RAT
AccessioniPrimary (citable) accession number: P15800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 113 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.