O15230 (LAMA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Laminin subunit alpha-5

Alternative name(s):
Laminin-10 subunit alpha
Laminin-11 subunit alpha
Laminin-15 subunit alpha

Gene names

Name:	LAMA5
Synonyms:	KIAA0533, KIAA1907

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3695 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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-5 is a subunit of laminin-10 (laminin-511), laminin-11 (laminin-521) and laminin-15 (laminin-523).
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane. Note: Major component.
Tissue specificity	Expressed in heart, lung, kidney, skeletal muscle, pancreas, retina and placenta. Little or no expression in brain and liver.
Domain	Domain G is globular and is part of the major cell-binding site located in the long arm of the laminin heterotrimer.
Sequence similarities	Contains 22 laminin EGF-like domains. Contains 5 laminin G-like domains. Contains 1 laminin IV type A domain. Contains 1 laminin N-terminal domain.
Sequence caution	The sequence CAC22310.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Non-traceable author statement Ref.1. Source: UniProtKB branching involved in salivary gland morphogenesis Inferred from electronic annotation. Source: Compara branching involved in ureteric bud morphogenesis Inferred from electronic annotation. Source: Compara cell migration Inferred from direct assay Ref.1. Source: UniProtKB cell proliferation Non-traceable author statement Ref.1. Source: UniProtKB cell recognition Non-traceable author statement Ref.1. Source: UniProtKB cilium assembly Inferred from electronic annotation. Source: Compara cytoskeleton organization Non-traceable author statement Ref.1. Source: UniProtKB embryo development Non-traceable author statement Ref.1. Source: UniProtKB endothelial cell differentiation Non-traceable author statement Ref.1. Source: UniProtKB establishment of protein localization to plasma membrane Inferred from electronic annotation. Source: Compara focal adhesion assembly Non-traceable author statement Ref.1. Source: UniProtKB hair follicle development Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from mutant phenotype Ref.1. Source: UniProtKB lung development Inferred from electronic annotation. Source: Compara morphogenesis of a polarized epithelium Inferred from electronic annotation. Source: Compara morphogenesis of embryonic epithelium Inferred from electronic annotation. Source: Compara muscle organ development Inferred from electronic annotation. Source: Compara neural crest cell migration Inferred from electronic annotation. Source: Compara odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from electronic annotation. Source: InterPro regulation of cell migration Inferred from electronic annotation. Source: InterPro regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of embryonic development Inferred from electronic annotation. Source: InterPro substrate adhesion-dependent cell spreading Inferred from direct assay PubMed 16236823. Source: BHF-UCL
Cellular_component	extracellular space Inferred from direct assay PubMed 10964500. Source: UniProtKB laminin-1 complex Inferred from electronic annotation. Source: InterPro laminin-10 complex Inferred from direct assay PubMed 10964500. Source: UniProtKB laminin-11 complex Traceable author statement PubMed 16236823. Source: BHF-UCL
Molecular_function	integrin binding Inferred from direct assay Ref.1. Source: UniProtKB structural molecule activity Inferred by curator Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 3695	3660	Laminin subunit alpha-5		PRO_0000017062
Regions
	Domain	41 – 299	259	Laminin N-terminal
	Domain	300 – 358	59	Laminin EGF-like 1
	Domain	359 – 428	70	Laminin EGF-like 2
	Domain	429 – 474	46	Laminin EGF-like 3
	Domain	494 – 540	47	Laminin EGF-like 4
	Domain	541 – 586	46	Laminin EGF-like 5
	Domain	587 – 631	45	Laminin EGF-like 6
	Domain	632 – 676	45	Laminin EGF-like 7
	Domain	677 – 722	46	Laminin EGF-like 8
	Domain	723 – 775	53	Laminin EGF-like 9
	Domain	776 – 828	53	Laminin EGF-like 10
	Domain	829 – 850	22	Laminin EGF-like 11; truncated
	Domain	1438 – 1483	46	Laminin EGF-like 12
	Domain	1484 – 1527	44	Laminin EGF-like 13
	Domain	1528 – 1576	49	Laminin EGF-like 14
	Domain	1577 – 1627	51	Laminin EGF-like 15
	Domain	1628 – 1637	10	Laminin EGF-like 16; first part
	Domain	1641 – 1830	190	Laminin IV type A
	Domain	1831 – 1863	33	Laminin EGF-like 16; second part
	Domain	1864 – 1912	49	Laminin EGF-like 17
	Domain	1913 – 1968	56	Laminin EGF-like 18
	Domain	1969 – 2022	54	Laminin EGF-like 19
	Domain	2023 – 2069	47	Laminin EGF-like 20
	Domain	2070 – 2116	47	Laminin EGF-like 21
	Domain	2117 – 2166	50	Laminin EGF-like 22
	Domain	2736 – 2929	194	Laminin G-like 1
	Domain	2941 – 3115	175	Laminin G-like 2
	Domain	3124 – 3292	169	Laminin G-like 3
	Domain	3340 – 3513	174	Laminin G-like 4
	Domain	3520 – 3692	173	Laminin G-like 5
	Region	851 – 1437	587	Domain IV 1 (domain IV B)
	Region	2167 – 2735	569	Domain II and I
	Coiled coil	2203 – 2221	19	Potential
	Coiled coil	2335 – 2466	132	Potential
	Coiled coil	2510 – 2670	161	Potential
	Motif	1722 – 1724	3	Cell attachment site Potential
	Motif	1838 – 1840	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	143	1	N-linked (GlcNAc...) Potential
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Glycosylation	452	1	N-linked (GlcNAc...) Potential
	Glycosylation	479	1	N-linked (GlcNAc...) Potential
	Glycosylation	900	1	N-linked (GlcNAc...) Potential
	Glycosylation	921	1	N-linked (GlcNAc...) Potential
	Glycosylation	959	1	N-linked (GlcNAc...) Potential
	Glycosylation	1330	1	N-linked (GlcNAc...) Potential
	Glycosylation	1529	1	N-linked (GlcNAc...) Potential
	Glycosylation	1555	1	N-linked (GlcNAc...) Potential
	Glycosylation	2196	1	N-linked (GlcNAc...) Potential
	Glycosylation	2209	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2303	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2423	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2501	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2568	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2707	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	3107	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	3209	1	N-linked (GlcNAc...) Potential
	Glycosylation	3257	1	N-linked (GlcNAc...) Potential
	Glycosylation	3287	1	N-linked (GlcNAc...) Potential
	Glycosylation	3626	1	N-linked (GlcNAc...) Potential
	Disulfide bond	300 ↔ 309		By similarity
	Disulfide bond	302 ↔ 322		By similarity
	Disulfide bond	324 ↔ 333		By similarity
	Disulfide bond	336 ↔ 356		By similarity
	Disulfide bond	359 ↔ 368		By similarity
	Disulfide bond	361 ↔ 393		By similarity
	Disulfide bond	396 ↔ 405		By similarity
	Disulfide bond	408 ↔ 426		By similarity
	Disulfide bond	429 ↔ 440		By similarity
	Disulfide bond	431 ↔ 447		By similarity
	Disulfide bond	449 ↔ 458		By similarity
	Disulfide bond	461 ↔ 471		By similarity
	Disulfide bond	494 ↔ 506		By similarity
	Disulfide bond	496 ↔ 515		By similarity
	Disulfide bond	517 ↔ 526		By similarity
	Disulfide bond	529 ↔ 538		By similarity
	Disulfide bond	541 ↔ 553		By similarity
	Disulfide bond	543 ↔ 560		By similarity
	Disulfide bond	562 ↔ 571		By similarity
	Disulfide bond	574 ↔ 584		By similarity
	Disulfide bond	587 ↔ 599		By similarity
	Disulfide bond	589 ↔ 605		By similarity
	Disulfide bond	607 ↔ 616		By similarity
	Disulfide bond	619 ↔ 629		By similarity
	Disulfide bond	632 ↔ 644		By similarity
	Disulfide bond	634 ↔ 650		By similarity
	Disulfide bond	652 ↔ 661		By similarity
	Disulfide bond	664 ↔ 674		By similarity
	Disulfide bond	677 ↔ 689		By similarity
	Disulfide bond	679 ↔ 696		By similarity
	Disulfide bond	698 ↔ 707		By similarity
	Disulfide bond	710 ↔ 725		By similarity
	Disulfide bond	746 ↔ 755		By similarity
	Disulfide bond	758 ↔ 773		By similarity
	Disulfide bond	776 ↔ 790		By similarity
	Disulfide bond	778 ↔ 797		By similarity
	Disulfide bond	799 ↔ 808		By similarity
	Disulfide bond	811 ↔ 826		By similarity
	Disulfide bond	829 ↔ 841		By similarity
	Disulfide bond	831 ↔ 848		By similarity
	Disulfide bond	850 ↔ 859		By similarity
	Disulfide bond	1438 ↔ 1450		By similarity
	Disulfide bond	1440 ↔ 1457		By similarity
	Disulfide bond	1459 ↔ 1468		By similarity
	Disulfide bond	1471 ↔ 1481		By similarity
	Disulfide bond	1484 ↔ 1491		By similarity
	Disulfide bond	1486 ↔ 1498		By similarity
	Disulfide bond	1500 ↔ 1509		By similarity
	Disulfide bond	1512 ↔ 1525		By similarity
	Disulfide bond	1528 ↔ 1543		By similarity
	Disulfide bond	1530 ↔ 1550		By similarity
	Disulfide bond	1552 ↔ 1561		By similarity
	Disulfide bond	1564 ↔ 1574		By similarity
	Disulfide bond	1577 ↔ 1589		By similarity
	Disulfide bond	1579 ↔ 1596		By similarity
	Disulfide bond	1598 ↔ 1607		By similarity
	Disulfide bond	1610 ↔ 1625		By similarity
	Disulfide bond	1864 ↔ 1873		By similarity
	Disulfide bond	1866 ↔ 1880		By similarity
	Disulfide bond	1883 ↔ 1892		By similarity
	Disulfide bond	1895 ↔ 1910		By similarity
	Disulfide bond	1913 ↔ 1928		By similarity
	Disulfide bond	1915 ↔ 1937		By similarity
	Disulfide bond	1939 ↔ 1948		By similarity
	Disulfide bond	1951 ↔ 1966		By similarity
	Disulfide bond	1969 ↔ 1984		By similarity
	Disulfide bond	1971 ↔ 1991		By similarity
	Disulfide bond	1994 ↔ 2003		By similarity
	Disulfide bond	2006 ↔ 2020		By similarity
	Disulfide bond	2023 ↔ 2033		By similarity
	Disulfide bond	2025 ↔ 2040		By similarity
	Disulfide bond	2042 ↔ 2051		By similarity
	Disulfide bond	2054 ↔ 2067		By similarity
	Disulfide bond	2070 ↔ 2081		By similarity
	Disulfide bond	2072 ↔ 2088		By similarity
	Disulfide bond	2090 ↔ 2099		By similarity
	Disulfide bond	2102 ↔ 2114		By similarity
	Disulfide bond	2117 ↔ 2124		By similarity
	Disulfide bond	2119 ↔ 2131		By similarity
	Disulfide bond	2133 ↔ 2142		By similarity
	Disulfide bond	2145 ↔ 2164		By similarity
	Disulfide bond	2167		Interchain Probable
	Disulfide bond	2170		Interchain Probable
	Disulfide bond	2899 ↔ 2929		By similarity
	Disulfide bond	3090 ↔ 3115		By similarity
	Disulfide bond	3261 ↔ 3292		By similarity
	Disulfide bond	3490 ↔ 3513		By similarity
	Disulfide bond	3664 ↔ 3692		By similarity
Natural variations
	Natural variant	401	1	T → A. Ref.1 Corresponds to variant rs4925229 [ dbSNP | Ensembl ].		VAR_047887
	Natural variant	889	1	V → M. Ref.3 Corresponds to variant rs6062223 [ dbSNP | Ensembl ].		VAR_030847
	Natural variant	1258	1	M → T. Ref.1 Corresponds to variant rs3810548 [ dbSNP | Ensembl ].		VAR_030848
	Natural variant	1367	1	K → E. Ref.1 Ref.3 Corresponds to variant rs2427286 [ dbSNP | Ensembl ].		VAR_030849
	Natural variant	1434	1	G → A. Corresponds to variant rs17750870 [ dbSNP | Ensembl ].		VAR_030850
	Natural variant	1667	1	R → W. Corresponds to variant rs13039398 [ dbSNP | Ensembl ].		VAR_030851
	Natural variant	1671	1	T → M. Corresponds to variant rs944893 [ dbSNP | Ensembl ].		VAR_047888
	Natural variant	1717	1	H → Y. Corresponds to variant rs875379 [ dbSNP | Ensembl ].		VAR_030852
	Natural variant	1807	1	F → S. Ref.1 Ref.3 Corresponds to variant rs2427284 [ dbSNP | Ensembl ].		VAR_030853
	Natural variant	1900	1	V → M. Ref.1 Corresponds to variant rs2427283 [ dbSNP | Ensembl ].		VAR_030854
	Natural variant	1908	1	A → T. Corresponds to variant rs11698080 [ dbSNP | Ensembl ].		VAR_030855
	Natural variant	2036	1	H → R. Corresponds to variant rs6143021 [ dbSNP | Ensembl ].		VAR_030856
	Natural variant	2053	1	R → H. Corresponds to variant rs3737137 [ dbSNP | Ensembl ].		VAR_030857
	Natural variant	2062	1	D → N. Ref.1 Ref.4 Corresponds to variant rs2274934 [ dbSNP | Ensembl ].		VAR_030858
	Natural variant	2226	1	R → H. Corresponds to variant rs2297587 [ dbSNP | Ensembl ].		VAR_030859
	Natural variant	3079	1	R → W. Ref.1 Ref.4 Ref.5 Corresponds to variant rs944895 [ dbSNP | Ensembl ].		VAR_030860
Experimental info
	Sequence conflict	956	1	T → A in AAM12527. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O15230 [UniParc]. Last modified January 11, 2011. Version 8. Checksum: B13C479B55282E3C	FASTA	3,695	399,737
	10 20 30 40 50 60 MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF NLAEGARIAA 70 80 90 100 110 120 SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG QYCDICTAAN SNKAHPASNA 130 140 150 160 170 180 IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ VFHVAYVLIK FANSPRPDLW VLERSMDFGR 190 200 210 220 230 240 TYQPWQFFAS SKRDCLERFG PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG 250 260 270 280 290 300 AMNFSYSPLL REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC 310 320 330 340 350 360 VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA NSANECQSCN 370 380 390 400 410 420 CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT TGVNCERCLP GFYRSPNHPL 430 440 450 460 470 480 DSPHVCRRCN CESDFTDGTC EDLTGRCYCR PNFSGERCDV CAEGFTGFPS CYPTPSSSND 490 500 510 520 530 540 TREQVLPAGQ IVNCDCSAAG TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP 550 560 570 580 590 600 CQCSSPGVAD DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD 610 620 630 640 650 660 EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC RCRPGYTGTA 670 680 690 700 710 720 CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP RVTGLRCDTC VPGAYNFPYC 730 740 750 760 770 780 EAGSCHPAGL APVDPALPEA QVPCMCRAHV EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL 790 800 810 820 830 840 RGTLGGVAEC QPGTGQCFCK PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS 850 860 870 880 890 900 CEPRTGVCRC RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN 910 920 930 940 950 960 FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE EGRSATCANC 970 980 990 1000 1010 1020 TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV EAEGVLLDYV VLLPSAYYEA 1030 1040 1050 1060 1070 1080 ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL PLDGFPSAAG LEALCRQDNS LPRPCPTEQL 1090 1100 1110 1120 1130 1140 SPSHPPLITC TGSDVDVQLQ VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL 1150 1160 1170 1180 1190 1200 SLHPCLYSTL CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV 1210 1220 1230 1240 1250 1260 EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH AQDLTPAMSP 1270 1280 1290 1300 1310 1320 AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA FLLHGYQPAH PTFPVEVLIN 1330 1340 1350 1360 1370 1380 AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA LLDVTHSELT VTVRVPKGRW LWLDYVLVVP 1390 1400 1410 1420 1430 1440 ENVYSFGYLR EEPLDKSYDF ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC 1450 1460 1470 1480 1490 1500 HEVGATGPTC EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC 1510 1520 1530 1540 1550 1560 PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC KCRPNVTGRR 1570 1580 1590 1600 1610 1620 CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE NVQGPKCDQC SLGTFSLDAA 1630 1640 1650 1660 1670 1680 NPKGCTRCFC FGATERCRSS SYTRQEFVDM EGWVLLSTDR QVVPHERQPG TEMLRADLRH 1690 1700 1710 1720 1730 1740 VPEAVPEAFP ELYWQAPPSY LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN 1750 1760 1770 1780 1790 1800 QMSITFLEPA YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS 1810 1820 1830 1840 1850 1860 QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY RDVKGLFLGR 1870 1880 1890 1900 1910 1920 CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV SSRDDPSAPC VSCPCPLSVP 1930 1940 1950 1960 1970 1980 SNNFAEGCVL RGGRTQCLCK PGYAGASCER CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL 1990 2000 2010 2020 2030 2040 FSDCDPLTGA CRGCLRHTTG PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC 2050 2060 2070 2080 2090 2100 LCKAGVTGRR CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR 2110 2120 2130 2140 2150 2160 ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ VPVPGGPVGH 2170 2180 2190 2200 2210 2220 SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM AWARLHRLNA SIADLQSQLR 2230 2240 2250 2260 2270 2280 SPLGPRHETA QQLEVLEQQS TSLGQDARRL GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA 2290 2300 2310 2320 2330 2340 AIRAVDRTLS ELMSQTGHLG LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA 2350 2360 2370 2380 2390 2400 ELAAAQRLLA RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE 2410 2420 2430 2440 2450 2460 LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA KEELERLAAS 2470 2480 2490 2500 2510 2520 LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL NLSSIILDVN QDRLTQRAIE 2530 2540 2550 2560 2570 2580 ASNAYSRILQ AVQAAEDAAG QALQQADHTW ATVVRQGLVD RAQQLLANST ALEEAMLQEQ 2590 2600 2610 2620 2630 2640 QRLGLVWAAL QGARTQLRDV RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ 2650 2660 2670 2680 2690 2700 DTATRVQSQL QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL 2710 2720 2730 2740 2750 2760 ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP RDLADLAAYT 2770 2780 2790 2800 2810 2820 ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR DKKVHWVYQL GEAGPAVLSI 2830 2840 2850 2860 2870 2880 DEDIGEQFAA VSLDRTLQFG HMSVTVERQM IQETKGDTVA PGAEGLLNLR PDDFVFYVGG 2890 2900 2910 2920 2930 2940 YPSTFTPPPL LRFPGYRGCI EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL 2950 2960 2970 2980 2990 3000 TDGSYLDGTG FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL 3010 3020 3030 3040 3050 3060 LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS VEQDNDLELA 3070 3080 3090 3100 3110 3120 DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY VDLKRLNTTG VSAGCTADLL 3130 3140 3150 3160 3170 3180 VGRAMTFHGH GFLRLALSNV APLTGNVYSG FGFHSAQDSA LLYYRASPDG LCQVSLQQGR 3190 3200 3210 3220 3230 3240 VSLQLLRTEV KTQAGFADGA PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG 3250 3260 3270 3280 3290 3300 PPRLLLGGLP ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT 3310 3320 3330 3340 3350 3360 PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH LEFVGILARH 3370 3380 3390 3400 3410 3420 RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH FVAQMEGLGT RLRAQSRQRS 3430 3440 3450 3460 3470 3480 RPGRWHKVSV RWEKNRILLV TDGARAWSQE GPHRQHQGAE HPQPHTLFVG GLPASSHSSK 3490 3500 3510 3520 3530 3540 LPVTVGFSGC VKRLRLHGRP LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL 3550 3560 3570 3580 3590 3600 PDVGLELEVR PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL 3610 3620 3630 3640 3650 3660 CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE PMAVQPWPPA 3670 3680 3690 YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells." Doi M., Thyboll J., Kortesmaa J., Jansson K., Iivanainen A., Parvardeh M., Timpl R., Hedin U., Swedenborg J., Tryggvason K. J. Biol. Chem. 277:12741-12748(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-401; THR-1258; GLU-1367; SER-1807; MET-1900; ASN-2062 AND TRP-3079.
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins." Nagase T., Kikuno R., Ohara O. DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1934, VARIANTS MET-889; GLU-1367 AND SER-1807. Tissue: Brain.
[4]	"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2051-3695, VARIANTS ASN-2062 AND TRP-3079. Tissue: Brain.
[5]	"Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation." Durkin M.E., Loechel F., Mattei M.-G., Gilpin B.J., Albrechtsen R., Wewer U.M. FEBS Lett. 411:296-300(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2743-3695, VARIANT TRP-3079. Tissue: Placenta.
[6]	"Laminin expression in adult and developing retinae: evidence of two novel CNS laminins." Libby R.T., Champliaud M.-F., Claudepierre T., Xu Y., Gibbons E.P., Koch M., Burgeson R.E., Hunter D.D., Brunken W.J. J. Neurosci. 20:6517-6528(2000) [PubMed] [Europe PMC] [Abstract] Cited for: EXPRESSION IN RETINA.
[7]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2209; ASN-2303; ASN-2423; ASN-2501; ASN-2568; ASN-2707 AND ASN-3107, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF443072 mRNA. Translation: AAM12527.1. AL354836 Genomic DNA. Translation: CAC22310.1. Sequence problems. AB067494 mRNA. Translation: BAB67800.1. AB011105 mRNA. Translation: BAA25459.1. Z95636 mRNA. Translation: CAB09137.1.
IPI	IPI00783665.
RefSeq	NP_005551.3. NM_005560.3.
UniGene	Hs.473256.
3D structure databases
ProteinModelPortal	O15230.
SMR	O15230. Positions 42-427.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15230. 7 interactions.
MINT	MINT-1183475.
STRING	9606.ENSP00000252999.
PTM databases
PhosphoSite	O15230.
Proteomic databases
PaxDb	O15230.
PRIDE	O15230.
Protocols and materials databases
DNASU	3911.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000252999; ENSP00000252999; ENSG00000130702.
GeneID	3911.
KEGG	hsa:3911.
UCSC	uc002ycq.3. human.
Organism-specific databases
CTD	3911.
GeneCards	GC20M060883.
H-InvDB	HIX0015978.
HGNC	HGNC:6485. LAMA5.
MIM	601033. gene.
neXtProt	NX_O15230.
PharmGKB	PA30274.
HUGE	Search... Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG292643.
HOGENOM	HOG000231235.
HOVERGEN	HBG052300.
InParanoid	O15230.
KO	K06240.
OMA	LRHTTGP.
OrthoDB	EOG4VHK5G.
Enzyme and pathway databases
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling. amb2_neutrophils_pathway. amb2 Integrin signaling. syndecan_1_pathway. Syndecan-1-mediated signaling events.
Gene expression databases
ArrayExpress	O15230.
Bgee	O15230.
CleanEx	HS_LAMA5.
Genevestigator	O15230.
GermOnline	ENSG00000130702. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 5 hits.
InterPro	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. IPR001368. TNFR/NGFR_Cys_rich_reg. [Graphical view]
Pfam	PF00052. Laminin_B. 1 hit. PF00053. Laminin_EGF. 19 hits. PF02210. Laminin_G_2. 5 hits. PF06008. Laminin_I. 1 hit. PF06009. Laminin_II. 1 hit. PF00055. Laminin_N. 1 hit. [Graphical view]
SMART	SM00180. EGF_Lam. 20 hits. SM00281. LamB. 1 hit. SM00282. LamG. 5 hits. SM00136. LamNT. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 5 hits.
PROSITE	PS00022. EGF_1. 19 hits. PS01186. EGF_2. 3 hits. PS01248. EGF_LAM_1. 19 hits. PS50027. EGF_LAM_2. 21 hits. PS50025. LAM_G_DOMAIN. 5 hits. PS51115. LAMININ_IVA. 1 hit. PS51117. LAMININ_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LAMA5. human.
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00015. Reteplase. DB00031. Tenecteplase.
GenomeRNAi	3911.
NextBio	15363.
SOURCE	Search...

Entry information

Entry name

LAMA5_HUMAN

Accession

Primary (citable) accession number: O15230
Secondary accession number(s): Q8TDF8, Q8WZA7, Q9H1P1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	January 11, 2011
Last modified:	April 3, 2013
This is version 138 of the entry and version 8 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.