Q16787 (LAMA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Laminin subunit alpha-3

Alternative name(s):
Epiligrin 170 kDa subunit
Short name=E170
Epiligrin subunit alpha
Kalinin subunit alpha
Laminin-5 subunit alpha
Laminin-6 subunit alpha
Laminin-7 subunit alpha
Nicein subunit alpha

Gene names

Name:	LAMA3
Synonyms:	LAMNA

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	3333 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. Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes.
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-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin).
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane. Note: Major component.
Tissue specificity	Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS.
Induction	Laminin-5 is up-regulated in wound sites of human skin.
Domain	The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. Domain G is globular.
Involvement in disease	Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Laryngoonychocutaneous syndrome (LOCS) [MIM:245660]: Autosomal recessive epithelial disorder confined to the Punjabi Muslim population. The condition is characterized by cutaneous erosions, nail dystrophy and exuberant vascular granulation tissue in certain epithelia, especially conjunctiva and larynx. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2
Sequence similarities	Contains 15 laminin EGF-like domains. Contains 5 laminin G-like domains. Contains 1 laminin IV type A domain. Contains 1 laminin N-terminal domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Epidermolysis bullosa
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW epidermis development Traceable author statement Ref.5. Source: ProtInc hemidesmosome assembly Traceable author statement. Source: Reactome regulation of cell adhesion Inferred from electronic annotation. Source: InterPro regulation of cell migration Inferred from electronic annotation. Source: InterPro regulation of embryonic development Inferred from electronic annotation. Source: InterPro
Cellular_component	basement membrane Traceable author statement Ref.5. Source: ProtInc laminin-1 complex Inferred from electronic annotation. Source: InterPro laminin-5 complex Inferred from electronic annotation. Source: Compara
Molecular_function	structural molecule activity Non-traceable author statement Ref.5. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q16787-2)

Also known as: B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q16787-1)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1620: Missing.
     1621-1665: LYFTETQRLT...CPPAYAGDSC → MGWLWIFGAA...QASYVEFRPS

Isoform 3 (identifier: Q16787-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 3333	3298	Laminin subunit alpha-3		PRO_0000017058
Regions
	Domain	43 – 298	256	Laminin N-terminal
	Domain	299 – 355	57	Laminin EGF-like 1
	Domain	356 – 425	70	Laminin EGF-like 2
	Domain	426 – 469	44	Laminin EGF-like 3
	Domain	491 – 535	45	Laminin EGF-like 4
	Domain	536 – 588	53	Laminin EGF-like 5
	Domain	590 – 630	41	Laminin EGF-like 6
	Domain	631 – 683	53	Laminin EGF-like 7
	Domain	684 – 728	45	Laminin EGF-like 8
	Domain	1266 – 1311	46	Laminin EGF-like 9
	Domain	1312 – 1355	44	Laminin EGF-like 10
	Domain	1356 – 1404	49	Laminin EGF-like 11
	Domain	1405 – 1455	51	Laminin EGF-like 12
	Domain	1476 – 1653	178	Laminin IV type A
	Domain	1687 – 1733	47	Laminin EGF-like 13
	Domain	1734 – 1786	53	Laminin EGF-like 14
	Domain	1787 – 1821	35	Laminin EGF-like 15; truncated
	Domain	2390 – 2591	202	Laminin G-like 1
	Domain	2598 – 2760	163	Laminin G-like 2
	Domain	2767 – 2927	161	Laminin G-like 3
	Domain	2986 – 3150	165	Laminin G-like 4
	Domain	3157 – 3330	174	Laminin G-like 5
	Region	298 – 728	431	Domain V
	Region	796 – 1265	470	Domain IV 1 (domain IV B)
	Region	1266 – 1465	200	Domain III B
	Region	1654 – 1821	168	Domain III A
	Region	1822 – 2389	568	Domain II and I
	Coiled coil	1852 – 1941	90	Potential
	Coiled coil	1987 – 2169	183	Potential
	Coiled coil	2322 – 2388	67	Potential
	Motif	2278 – 2280	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	142	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Glycosylation	2365	1	N-linked (GlcNAc...) Potential
	Glycosylation	2502	1	N-linked (GlcNAc...) Potential
	Glycosylation	2584	1	N-linked (GlcNAc...) Potential
	Disulfide bond	299 ↔ 308		By similarity
	Disulfide bond	301 ↔ 319		By similarity
	Disulfide bond	321 ↔ 330		By similarity
	Disulfide bond	333 ↔ 353		By similarity
	Disulfide bond	356 ↔ 365		By similarity
	Disulfide bond	358 ↔ 390		By similarity
	Disulfide bond	393 ↔ 402		By similarity
	Disulfide bond	405 ↔ 423		By similarity
	Disulfide bond	426 ↔ 436		By similarity
	Disulfide bond	428 ↔ 443		By similarity
	Disulfide bond	445 ↔ 454		By similarity
	Disulfide bond	457 ↔ 467		By similarity
	Disulfide bond	491 ↔ 503		By similarity
	Disulfide bond	493 ↔ 509		By similarity
	Disulfide bond	511 ↔ 520		By similarity
	Disulfide bond	523 ↔ 533		By similarity
	Disulfide bond	536 ↔ 548		By similarity
	Disulfide bond	538 ↔ 555		By similarity
	Disulfide bond	557 ↔ 566		By similarity
	Disulfide bond	569 ↔ 586		By similarity
	Disulfide bond	601 ↔ 610		By similarity
	Disulfide bond	613 ↔ 628		By similarity
	Disulfide bond	631 ↔ 645		By similarity
	Disulfide bond	633 ↔ 652		By similarity
	Disulfide bond	654 ↔ 663		By similarity
	Disulfide bond	666 ↔ 681		By similarity
	Disulfide bond	684 ↔ 696		By similarity
	Disulfide bond	686 ↔ 703		By similarity
	Disulfide bond	705 ↔ 714		By similarity
	Disulfide bond	1266 ↔ 1278		By similarity
	Disulfide bond	1268 ↔ 1285		By similarity
	Disulfide bond	1287 ↔ 1296		By similarity
	Disulfide bond	1299 ↔ 1309		By similarity
	Disulfide bond	1312 ↔ 1319		By similarity
	Disulfide bond	1314 ↔ 1326		By similarity
	Disulfide bond	1328 ↔ 1337		By similarity
	Disulfide bond	1340 ↔ 1353		By similarity
	Disulfide bond	1356 ↔ 1371		By similarity
	Disulfide bond	1358 ↔ 1378		By similarity
	Disulfide bond	1380 ↔ 1389		By similarity
	Disulfide bond	1392 ↔ 1402		By similarity
	Disulfide bond	1405 ↔ 1417		By similarity
	Disulfide bond	1407 ↔ 1424		By similarity
	Disulfide bond	1426 ↔ 1435		By similarity
	Disulfide bond	1438 ↔ 1453		By similarity
	Disulfide bond	1687 ↔ 1696		By similarity
	Disulfide bond	1689 ↔ 1703		By similarity
	Disulfide bond	1706 ↔ 1715		By similarity
	Disulfide bond	1718 ↔ 1731		By similarity
	Disulfide bond	1734 ↔ 1746		By similarity
	Disulfide bond	1736 ↔ 1755		By similarity
	Disulfide bond	1757 ↔ 1766		By similarity
	Disulfide bond	1769 ↔ 1784		By similarity
	Disulfide bond	1822		Interchain Probable
	Disulfide bond	1825		Interchain Probable
	Disulfide bond	2561 ↔ 2591		By similarity
	Disulfide bond	2737 ↔ 2760		By similarity
	Disulfide bond	2895 ↔ 2927		By similarity
	Disulfide bond	3127 ↔ 3150		By similarity
	Disulfide bond	3302 ↔ 3330		By similarity
Natural variations
	Alternative sequence	1 – 1620	1620	Missing in isoform 1.		VSP_035738
	Alternative sequence	1621 – 1665	45	LYFTE…AGDSC → MGWLWIFGAALGQCLGYSSQ QQRVPFLQPPGQSQLQASYV EFRPS in isoform 1.		VSP_035739
	Alternative sequence	1946 – 2002	57	ILLKQ…ESQLL → M in isoform 3.		VSP_043487
	Natural variant	796	1	T → N. Corresponds to variant rs17187262 [ dbSNP | Ensembl ].		VAR_050078
	Natural variant	1206	1	V → A. Corresponds to variant rs12457323 [ dbSNP | Ensembl ].		VAR_050079
	Natural variant	1208	1	P → T. Corresponds to variant rs17202961 [ dbSNP | Ensembl ].		VAR_050080
	Natural variant	1774	1	F → L. Corresponds to variant rs958631 [ dbSNP | Ensembl ].		VAR_059444
	Natural variant	2702	1	T → A. Corresponds to variant rs9952370 [ dbSNP | Ensembl ].		VAR_047374
	Natural variant	2815	1	N → K. Corresponds to variant rs1154232 [ dbSNP | Ensembl ].		VAR_047375
	Natural variant	2834	1	S → G. Ref.1 Ref.3 Ref.6 Corresponds to variant rs1154233 [ dbSNP | Ensembl ].		VAR_059445
Experimental info
	Sequence conflict	1544	1	G → A in CAA59429. Ref.5
	Sequence conflict	1544	1	G → A in CAA59325. Ref.6
	Sequence conflict	1743 – 1745	3	ATG → GMC in CAA59428. Ref.5
	Sequence conflict	1743 – 1745	3	ATG → GMC in CAA59429. Ref.5
	Sequence conflict	2101	1	M → K in CAA59428. Ref.5
	Sequence conflict	2101	1	M → K in CAA59429. Ref.5
	Sequence conflict	2374	1	R → L in CAA59428. Ref.5
	Sequence conflict	2374	1	R → L in CAA59429. Ref.5
	Sequence conflict	2589	1	E → Q in CAA59428. Ref.5
	Sequence conflict	2589	1	E → Q in CAA59429. Ref.5
	Sequence conflict	2672	1	D → A in CAA59428. Ref.5
	Sequence conflict	2672	1	D → A in CAA59429. Ref.5
	Sequence conflict	2804	1	G → A in CAA59428. Ref.5
	Sequence conflict	2804	1	G → A in CAA59429. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (B) [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 9F99AF49B8EF27DD	FASTA	3,333	366,649
	10 20 30 40 50 60 MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT YFNLAEAARI 70 80 90 100 110 120 WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ FCDYCNSEDP RKAHPVTNAI 130 140 150 160 170 180 DGSERWWQSP PLSSGTQYNR VNLTLDLGQL FHVAYILIKF ANSPRPDLWV LERSVDFGST 190 200 210 220 230 240 YSPWQYFAHS KVDCLKEFGR EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA 250 260 270 280 290 300 KNFTFSHTLR EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV 310 320 330 340 350 360 CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS HECEACNCHG 370 380 390 400 410 420 HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV NCEQCAKGYY RPYGVPVDAP 430 440 450 460 470 480 DGCIPCSCDP EHADGCEQGS GRCHCKPNFH GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS 490 500 510 520 530 540 EDPVAGDIKG CDCNLEGVLP EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA 550 560 570 580 590 600 LGSYQMPCSS VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ 610 620 630 640 650 660 CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG DCHCKSHVGG 670 680 690 700 710 720 DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS GVCQCREHVV GKVCQRPENN 730 740 750 760 770 780 YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP LAFPEFSWRG YAQMTSVQND VRITLNVGKS 790 800 810 820 830 840 SGSLFRVILR YVNPGTEAVS GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS 850 860 870 880 890 900 ITPGIWVACI KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT 910 920 930 940 950 960 RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI PQVGHYVVVV 970 980 990 1000 1010 1020 EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS AVIDHMSRIA MYELLADADI 1030 1040 1050 1060 1070 1080 QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ VHCIASYGRF VNQSATCVSL AHETPPTALI 1090 1100 1110 1120 1130 1140 LDVLSGRPFP HLPQQSSPSV DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT 1150 1160 1170 1180 1190 1200 FPAQVSVDGG WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV 1210 1220 1230 1240 1250 1260 LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN SARSLVAFYH 1270 1280 1290 1300 1310 1320 KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA TGHYGFPRCK PCSCGRRLCE 1330 1340 1350 1360 1370 1380 EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC 1390 1400 1410 1420 1430 1440 KPRITGRQCD RCASGFYRFP ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE 1450 1460 1470 1480 1490 1500 GSFHLDPANL KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN 1510 1520 1530 1540 1550 1560 SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV LLEKKPDVQL 1570 1580 1590 1600 1610 1620 TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP VSREELMTVL SRLADVRIQG 1630 1640 1650 1660 1670 1680 LYFTETQRLT LSEVGLEEAS DTGSGRIALA VEICACPPAY AGDSCQGCSP GYYRDHKGLY 1690 1700 1710 1720 1730 1740 TGRCVPCNCN GHSNQCQDGS GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN 1750 1760 1770 1780 1790 1800 SFATGCVVNG GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP 1810 1820 1830 1840 1850 1860 LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL SASAGLLEQM 1870 1880 1890 1900 1910 1920 RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ EFETLQEKAQ VNSRKAQTLN 1930 1940 1950 1960 1970 1980 NNVNRATQSA KELDVKIKNV IRNVHILLKQ ISGTDGEGNN VPSGDFSREW AEAQRMMREL 1990 2000 2010 2020 2030 2040 RNRNFGKHLR EAEADKRESQ LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA 2050 2060 2070 2080 2090 2100 RLQEAAAQAK QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL 2110 2120 2130 2140 2150 2160 MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ ELAKQLEEIK 2170 2180 2190 2200 2210 2220 RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS ESALQTVIKE DLPRKAKTLS 2230 2240 2250 2260 2270 2280 SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD 2290 2300 2310 2320 2330 2340 IDAMISSAKS MVRKANDITD EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN 2350 2360 2370 2380 2390 2400 KLTNKLPDLW RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE 2410 2420 2430 2440 2450 2460 VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG MAVVDGQLTC 2470 2480 2490 2500 2510 2520 VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR LNYTKGATSS KPETPGVYDM 2530 2540 2550 2560 2570 2580 DGRNSNTLLN LDPENVVFYV GGYPPDFKLP SRLSFPPYKG CIELDDLNEN VLSLYNFKKT 2590 2600 2610 2620 2630 2640 FNLNTTEVEP CRRRKEESDK NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN 2650 2660 2670 2680 2690 2700 GDRFISLNIE DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ 2710 2720 2730 2740 2750 2760 NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL NDTVGVTKKC 2770 2780 2790 2800 2810 2820 SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF QPSGILLDHQ TWTRNLQVTL 2830 2840 2850 2860 2870 2880 EDGYIELSTS DSGSPIFKSP QTYMDGLLHY VSVISDNSGL RLLIDDQLLR NSKRLKHISS 2890 2900 2910 2920 2930 2940 SRQSLRLGGS NFEGCISNVF VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG 2950 2960 2970 2980 2990 3000 STRFNKTKTF RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK 3010 3020 3030 3040 3050 3060 LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT DGKKLRIKSK 3070 3080 3090 3100 3110 3120 EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI SIRAPVYLGS PPSGKPKSLP 3130 3140 3150 3160 3170 3180 TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF 3190 3200 3210 3220 3230 3240 KLVFSIRPRS LTGILIHIGS QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ 3250 3260 3270 3280 3290 3300 WHSVAVTIKQ HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF 3310 3320 3330 GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ
	Isoform 1 (A) [UniParc]. Checksum: B5EA9BE5F20DBBBE	FASTA	1,713	189,335
	10 20 30 40 50 60 MGWLWIFGAA LGQCLGYSSQ QQRVPFLQPP GQSQLQASYV EFRPSQGCSP GYYRDHKGLY 70 80 90 100 110 120 TGRCVPCNCN GHSNQCQDGS GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN 130 140 150 160 170 180 SFATGCVVNG GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP 190 200 210 220 230 240 LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL SASAGLLEQM 250 260 270 280 290 300 RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ EFETLQEKAQ VNSRKAQTLN 310 320 330 340 350 360 NNVNRATQSA KELDVKIKNV IRNVHILLKQ ISGTDGEGNN VPSGDFSREW AEAQRMMREL 370 380 390 400 410 420 RNRNFGKHLR EAEADKRESQ LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA 430 440 450 460 470 480 RLQEAAAQAK QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL 490 500 510 520 530 540 MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ ELAKQLEEIK 550 560 570 580 590 600 RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS ESALQTVIKE DLPRKAKTLS 610 620 630 640 650 660 SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD 670 680 690 700 710 720 IDAMISSAKS MVRKANDITD EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN 730 740 750 760 770 780 KLTNKLPDLW RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE 790 800 810 820 830 840 VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG MAVVDGQLTC 850 860 870 880 890 900 VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR LNYTKGATSS KPETPGVYDM 910 920 930 940 950 960 DGRNSNTLLN LDPENVVFYV GGYPPDFKLP SRLSFPPYKG CIELDDLNEN VLSLYNFKKT 970 980 990 1000 1010 1020 FNLNTTEVEP CRRRKEESDK NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN 1030 1040 1050 1060 1070 1080 GDRFISLNIE DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ 1090 1100 1110 1120 1130 1140 NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL NDTVGVTKKC 1150 1160 1170 1180 1190 1200 SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF QPSGILLDHQ TWTRNLQVTL 1210 1220 1230 1240 1250 1260 EDGYIELSTS DSGSPIFKSP QTYMDGLLHY VSVISDNSGL RLLIDDQLLR NSKRLKHISS 1270 1280 1290 1300 1310 1320 SRQSLRLGGS NFEGCISNVF VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG 1330 1340 1350 1360 1370 1380 STRFNKTKTF RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK 1390 1400 1410 1420 1430 1440 LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT DGKKLRIKSK 1450 1460 1470 1480 1490 1500 EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI SIRAPVYLGS PPSGKPKSLP 1510 1520 1530 1540 1550 1560 TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF 1570 1580 1590 1600 1610 1620 KLVFSIRPRS LTGILIHIGS QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ 1630 1640 1650 1660 1670 1680 WHSVAVTIKQ HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF 1690 1700 1710 GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ
	Isoform 3 [UniParc]. Checksum: 3ACFFE998357122E	FASTA	3,277	360,212
	10 20 30 40 50 60 MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT YFNLAEAARI 70 80 90 100 110 120 WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ FCDYCNSEDP RKAHPVTNAI 130 140 150 160 170 180 DGSERWWQSP PLSSGTQYNR VNLTLDLGQL FHVAYILIKF ANSPRPDLWV LERSVDFGST 190 200 210 220 230 240 YSPWQYFAHS KVDCLKEFGR EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA 250 260 270 280 290 300 KNFTFSHTLR EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV 310 320 330 340 350 360 CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS HECEACNCHG 370 380 390 400 410 420 HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV NCEQCAKGYY RPYGVPVDAP 430 440 450 460 470 480 DGCIPCSCDP EHADGCEQGS GRCHCKPNFH GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS 490 500 510 520 530 540 EDPVAGDIKG CDCNLEGVLP EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA 550 560 570 580 590 600 LGSYQMPCSS VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ 610 620 630 640 650 660 CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG DCHCKSHVGG 670 680 690 700 710 720 DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS GVCQCREHVV GKVCQRPENN 730 740 750 760 770 780 YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP LAFPEFSWRG YAQMTSVQND VRITLNVGKS 790 800 810 820 830 840 SGSLFRVILR YVNPGTEAVS GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS 850 860 870 880 890 900 ITPGIWVACI KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT 910 920 930 940 950 960 RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI PQVGHYVVVV 970 980 990 1000 1010 1020 EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS AVIDHMSRIA MYELLADADI 1030 1040 1050 1060 1070 1080 QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ VHCIASYGRF VNQSATCVSL AHETPPTALI 1090 1100 1110 1120 1130 1140 LDVLSGRPFP HLPQQSSPSV DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT 1150 1160 1170 1180 1190 1200 FPAQVSVDGG WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV 1210 1220 1230 1240 1250 1260 LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN SARSLVAFYH 1270 1280 1290 1300 1310 1320 KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA TGHYGFPRCK PCSCGRRLCE 1330 1340 1350 1360 1370 1380 EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC 1390 1400 1410 1420 1430 1440 KPRITGRQCD RCASGFYRFP ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE 1450 1460 1470 1480 1490 1500 GSFHLDPANL KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN 1510 1520 1530 1540 1550 1560 SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV LLEKKPDVQL 1570 1580 1590 1600 1610 1620 TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP VSREELMTVL SRLADVRIQG 1630 1640 1650 1660 1670 1680 LYFTETQRLT LSEVGLEEAS DTGSGRIALA VEICACPPAY AGDSCQGCSP GYYRDHKGLY 1690 1700 1710 1720 1730 1740 TGRCVPCNCN GHSNQCQDGS GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN 1750 1760 1770 1780 1790 1800 SFATGCVVNG GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP 1810 1820 1830 1840 1850 1860 LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL SASAGLLEQM 1870 1880 1890 1900 1910 1920 RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ EFETLQEKAQ VNSRKAQTLN 1930 1940 1950 1960 1970 1980 NNVNRATQSA KELDVKIKNV IRNVHMLNRI RTWQKTHQGE NNGLANSIRD SLNEYEAKLS 1990 2000 2010 2020 2030 2040 DLRARLQEAA AQAKQANGLN QENERALGAI QRQVKEINSL QSDFTKYLTT ADSSLLQTNI 2050 2060 2070 2080 2090 2100 ALQLMEKSQK EYEKLAASLN EARQELSDKV RELSRSAGKT SLVEEAEKHA RSLQELAKQL 2110 2120 2130 2140 2150 2160 EEIKRNASGD ELVRCAVDAA TAYENILNAI KAAEDAANRA ASASESALQT VIKEDLPRKA 2170 2180 2190 2200 2210 2220 KTLSSNSDKL LNEAKMTQKK LKQEVSPALN NLQQTLNIVT VQKEVIDTNL TTLRDGLHGI 2230 2240 2250 2260 2270 2280 QRGDIDAMIS SAKSMVRKAN DITDEVLDGL NPIQTDVERI KDTYGRTQNE DFKKALTDAD 2290 2300 2310 2320 2330 2340 NSVNKLTNKL PDLWRKIESI NQQLLPLGNI SDNMDRIREL IQQARDAASK VAVPMRFNGK 2350 2360 2370 2380 2390 2400 SGVEVRLPND LEDLKGYTSL SLFLQRPNSR ENGGTENMFV MYLGNKDASR DYIGMAVVDG 2410 2420 2430 2440 2450 2460 QLTCVYNLGD REAELQVDQI LTKSETKEAV MDRVKFQRIY QFARLNYTKG ATSSKPETPG 2470 2480 2490 2500 2510 2520 VYDMDGRNSN TLLNLDPENV VFYVGGYPPD FKLPSRLSFP PYKGCIELDD LNENVLSLYN 2530 2540 2550 2560 2570 2580 FKKTFNLNTT EVEPCRRRKE ESDKNYFEGT GYARVPTQPH APIPTFGQTI QTTVDRGLLF 2590 2600 2610 2620 2630 2640 FAENGDRFIS LNIEDGKLMV RYKLNSELPK ERGVGDAINN GRDHSIQIKI GKLQKRMWIN 2650 2660 2670 2680 2690 2700 VDVQNTIIDG EVFDFSTYYL GGIPIAIRER FNISTPAFRG CMKNLKKTSG VVRLNDTVGV 2710 2720 2730 2740 2750 2760 TKKCSEDWKL VRSASFSRGG QLSFTDLGLP PTDHLQASFG FQTFQPSGIL LDHQTWTRNL 2770 2780 2790 2800 2810 2820 QVTLEDGYIE LSTSDSGSPI FKSPQTYMDG LLHYVSVISD NSGLRLLIDD QLLRNSKRLK 2830 2840 2850 2860 2870 2880 HISSSRQSLR LGGSNFEGCI SNVFVQRLSL SPEVLDLTSN SLKRDVSLGG CSLNKPPFLM 2890 2900 2910 2920 2930 2940 LLKGSTRFNK TKTFRINQLL QDTPVASPRS VKVWQDACSP LPKTQANHGA LQFGDIPTSH 2950 2960 2970 2980 2990 3000 LLFKLPQELL KPRSQFAVDM QTTSSRGLVF HTGTKNSFMA LYLSKGRLVF ALGTDGKKLR 3010 3020 3030 3040 3050 3060 IKSKEKCNDG KWHTVVFGHD GEKGRLVVDG LRAREGSLPG NSTISIRAPV YLGSPPSGKP 3070 3080 3090 3100 3110 3120 KSLPTNSFVG CLKNFQLDSK PLYTPSSSFG VSSCLGGPLE KGIYFSEEGG HVVLAHSVLL 3130 3140 3150 3160 3170 3180 GPEFKLVFSI RPRSLTGILI HIGSQPGKHL CVYLEAGKVT ASMDSGAGGT STSVTPKQSL 3190 3200 3210 3220 3230 3240 CDGQWHSVAV TIKQHILHLE LDTDSSYTAG QIPFPPASTQ EPLHLGGAPA NLTTLRIPVW 3250 3260 3270 KSFFGCLRNI HVNHIPVPVT EALEVQGPVS LNGCPDQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair." Ryan M.C., Tizard R., Vandevanter D.R., Carter W.G. J. Biol. Chem. 269:22779-22787(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-2834. Tissue: Keratinocyte.
[2]	"An unusual N-terminal deletion of the laminin alpha3a isoform leads to the chronic granulation tissue disorder laryngo-onycho-cutaneous syndrome." McLean W.H.I., Irvine A.D., Hamill K.J., Whittock N.V., Coleman-Campbell C.M., Mellerio J.E., Ashton G.S., Dopping-Hepenstal P.J.H., Eady R.A.J., Jamil T., Phillips R.J., Shabbir S.G., Haroon T.S., Khurshid K., Moore J.E., Page B., Darling J., Atherton D.J. , Van Steensel M.A.M., Munro C.S., Smith F.J.D., McGrath J.A. Hum. Mol. Genet. 12:2395-2409(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), DISEASE.
[3]	"Characterization of laminin 5B and NH2-terminal proteolytic fragment of its alpha3B chain: promotion of cellular adhesion, migration, and proliferation." Kariya Y., Yasuda C., Nakashima Y., Ishida K., Tsubota Y., Miyazaki K. J. Biol. Chem. 279:24774-24784(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT GLY-2834.
[4]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa." Vidal F., Baudoin C., Miquel C., Galliano M.-F., Christiano A.M., Uitto J., Ortonne J.-P., Meneguzzi G. Genomics 30:273-280(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2858 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1528-2858 (ISOFORMS 1/2). Tissue: Keratinocyte.
[6]	"Mutation in LAMA3 gene in a patient affected by H-Jeb." Aberdam D., Vidal F., Baudoin C., Miquel C., Ortonne J.-P., Meneguzzi G. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1528-3333 (ISOFORMS 1/2), VARIANT GLY-2834.
[7]	"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.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	L34155 mRNA. Translation: AAA59483.1. AY327115 mRNA. Translation: AAQ72570.1. AY327116 mRNA. Translation: AAQ72571.1. AB107369 Genomic DNA. Translation: BAD13428.1. AC010754 Genomic DNA. No translation available. AC067796 Genomic DNA. No translation available. AC090366 Genomic DNA. No translation available. X85107 mRNA. Translation: CAA59428.1. X85108 mRNA. Translation: CAA59429.1. X84900 mRNA. Translation: CAA59325.1.
IPI	IPI00377045. IPI00743994. IPI00790908.
PIR	A55347.
RefSeq	NP_000218.2. NM_000227.3. NP_001121189.1. NM_001127717.1. NP_937762.1. NM_198129.1.
UniGene	Hs.436367.
3D structure databases
ProteinModelPortal	Q16787.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16787. 3 interactions.
MINT	MINT-1431248.
STRING	9606.ENSP00000324532.
PTM databases
PhosphoSite	Q16787.
Polymorphism databases
DMDM	215274012.
Proteomic databases
PaxDb	Q16787.
PRIDE	Q16787.
Protocols and materials databases
DNASU	3909.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000313654; ENSP00000324532; ENSG00000053747. ENST00000399516; ENSP00000382432; ENSG00000053747.
GeneID	3909.
KEGG	hsa:3909.
UCSC	uc002kuq.3. human.
Organism-specific databases
CTD	3909.
GeneCards	GC18P021269.
HGNC	HGNC:6483. LAMA3.
HPA	CAB010757. HPA009309.
MIM	226700. phenotype. 245660. phenotype. 600805. gene.
neXtProt	NX_Q16787.
Orphanet	79402. Generalized junctional epidermolysis bullosa, non-Herlitz type. 79404. Junctional epidermolysis bullosa, Herlitz type. 2407. LOGIC syndrome.
PharmGKB	PA30272.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG292643.
HOGENOM	HOG000231235.
HOVERGEN	HBG052300.
KO	K06240.
OMA	DSCQGCS.
OrthoDB	EOG4FBHS0.
Enzyme and pathway databases
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling. amb2_neutrophils_pathway. amb2 Integrin signaling. syndecan_2_pathway. Syndecan-2-mediated signaling events. syndecan_4_pathway. Syndecan-4-mediated signaling events.
Reactome	REACT_111102. Signal Transduction. REACT_111155. Cell-Cell communication. REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q16787.
Bgee	Q16787.
CleanEx	HS_LAMA3.
Genevestigator	Q16787.
GermOnline	ENSG00000053747. 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. IPR009030. Growth_fac_rcpt. IPR018031. Laminin_B_subgr. IPR000034. Laminin_B_type_IV. IPR001791. Laminin_G. IPR009254. Laminin_I. IPR010307. Laminin_II. IPR008211. Laminin_N. [Graphical view]
Pfam	PF00052. Laminin_B. 1 hit. PF00053. Laminin_EGF. 12 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. 14 hits. SM00281. LamB. 1 hit. SM00282. LamG. 5 hits. SM00136. LamNT. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 5 hits. SSF57184. Grow_fac_recept. 1 hit.
PROSITE	PS00022. EGF_1. 12 hits. PS01186. EGF_2. 1 hit. PS01248. EGF_LAM_1. 13 hits. PS50027. EGF_LAM_2. 14 hits. PS50025. LAM_G_DOMAIN. 5 hits. PS51115. LAMININ_IVA. 1 hit. PS51117. LAMININ_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LAMA3. human.
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00015. Reteplase. DB00031. Tenecteplase.
GenomeRNAi	3909.
NextBio	15345.
PMAP-CutDB	Q6VU68.
SOURCE	Search...

Entry information

Entry name

LAMA3_HUMAN

Accession

Primary (citable) accession number: Q16787
Secondary accession number(s): Q13679 , Q13680, Q6VU67, Q6VU68, Q76E14, Q96TG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 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.