Q9Y6N6 (LAMC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Laminin subunit gamma-3

Alternative name(s):
Laminin-12 subunit gamma
Laminin-14 subunit gamma
Laminin-15 subunit gamma

Gene names

Name:

LAMC3

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	1575 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. Gamma-3 is a subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and laminin-15 (laminin-523).
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane.
Tissue specificity	Broadly expressed in: skin, heart, lung, and the reproductive tracts.
Domain	The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. Domain IV is globular.
Involvement in disease	Cortical malformations occipital (OCCM) [MIM:614115]: A disease in which affected individuals develop seizures, sometimes associated with transient visual changes. Brain MRI shows both pachygyria and polymicrogyria restricted to the lateral occipital lobes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4
Sequence similarities	Contains 11 laminin EGF-like domains. Contains 1 laminin IV type A domain. Contains 1 laminin N-terminal domain.
Sequence caution	The sequence AAD36991.1 differs from that shown. Reason: Frameshift at positions 598 and 609.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	astrocyte development Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell morphogenesis involved in differentiation Inferred from electronic annotation. Source: Compara retina development in camera-type eye Inferred from electronic annotation. Source: Compara visual perception Inferred from electronic annotation. Source: Compara
Cellular_component	basement membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Traceable author statement Ref.1. Source: ProtInc proteinaceous extracellular matrix Traceable author statement Ref.1. Source: ProtInc
Molecular_function	structural molecule activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 1575	1556	Laminin subunit gamma-3		PRO_0000017079
Regions
	Domain	31 – 270	240	Laminin N-terminal
	Domain	271 – 326	56	Laminin EGF-like 1
	Domain	327 – 382	56	Laminin EGF-like 2
	Domain	383 – 429	47	Laminin EGF-like 3
	Domain	430 – 479	50	Laminin EGF-like 4
	Domain	480 – 489	10	Laminin EGF-like 5; first part
	Domain	499 – 672	174	Laminin IV type A
	Domain	673 – 706	34	Laminin EGF-like 5; second part
	Domain	707 – 754	48	Laminin EGF-like 6
	Domain	755 – 809	55	Laminin EGF-like 7
	Domain	810 – 865	56	Laminin EGF-like 8
	Domain	866 – 916	51	Laminin EGF-like 9
	Domain	917 – 964	48	Laminin EGF-like 10
	Domain	965 – 1013	49	Laminin EGF-like 11
	Region	1014 – 1575	562	Domain II and I
	Coiled coil	1073 – 1134	62	Potential
	Coiled coil	1201 – 1228	28	Potential
	Coiled coil	1410 – 1492	83	Potential
	Coiled coil	1523 – 1567	45	Potential
	Motif	1059 – 1061	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	87	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	295	1	N-linked (GlcNAc...) Potential
	Glycosylation	328	1	N-linked (GlcNAc...) Potential
	Glycosylation	631	1	N-linked (GlcNAc...) Potential
	Glycosylation	837	1	N-linked (GlcNAc...) Potential
	Glycosylation	980	1	N-linked (GlcNAc...) Potential
	Glycosylation	1185	1	N-linked (GlcNAc...) Potential
	Disulfide bond	271 ↔ 280		By similarity
	Disulfide bond	273 ↔ 290		By similarity
	Disulfide bond	292 ↔ 301		By similarity
	Disulfide bond	304 ↔ 324		By similarity
	Disulfide bond	327 ↔ 336		By similarity
	Disulfide bond	329 ↔ 352		By similarity
	Disulfide bond	355 ↔ 364		By similarity
	Disulfide bond	367 ↔ 380		By similarity
	Disulfide bond	383 ↔ 395		By similarity
	Disulfide bond	385 ↔ 401		By similarity
	Disulfide bond	403 ↔ 412		By similarity
	Disulfide bond	415 ↔ 427		By similarity
	Disulfide bond	430 ↔ 441		By similarity
	Disulfide bond	432 ↔ 448		By similarity
	Disulfide bond	450 ↔ 459		By similarity
	Disulfide bond	462 ↔ 477		By similarity
	Disulfide bond	707 ↔ 715		By similarity
	Disulfide bond	709 ↔ 722		By similarity
	Disulfide bond	724 ↔ 733		By similarity
	Disulfide bond	736 ↔ 752		By similarity
	Disulfide bond	755 ↔ 763		By similarity
	Disulfide bond	757 ↔ 774		By similarity
	Disulfide bond	777 ↔ 786		By similarity
	Disulfide bond	789 ↔ 807		By similarity
	Disulfide bond	810 ↔ 824		By similarity
	Disulfide bond	812 ↔ 831		By similarity
	Disulfide bond	834 ↔ 843		By similarity
	Disulfide bond	846 ↔ 863		By similarity
	Disulfide bond	866 ↔ 880		By similarity
	Disulfide bond	868 ↔ 887		By similarity
	Disulfide bond	889 ↔ 898		By similarity
	Disulfide bond	901 ↔ 914		By similarity
	Disulfide bond	917 ↔ 929		By similarity
	Disulfide bond	919 ↔ 936		By similarity
	Disulfide bond	938 ↔ 947		By similarity
	Disulfide bond	950 ↔ 962		By similarity
	Disulfide bond	965 ↔ 977		By similarity
	Disulfide bond	967 ↔ 983		By similarity
	Disulfide bond	985 ↔ 994		By similarity
	Disulfide bond	997 ↔ 1010		By similarity
Natural variations
	Natural variant	350	1	G → R in OCCM. Ref.4		VAR_066404
	Natural variant	522	1	P → S. Ref.1 Corresponds to variant rs869457 [ dbSNP | Ensembl ].		VAR_056145
	Natural variant	544	1	E → G. Ref.1 Ref.3 Corresponds to variant rs10901333 [ dbSNP | Ensembl ].		VAR_056146
	Natural variant	770	1	R → G. Ref.1 Ref.3 Corresponds to variant rs3739510 [ dbSNP | Ensembl ].		VAR_056147
	Natural variant	1082	1	S → G. Ref.1 Ref.3 Corresponds to variant rs2275140 [ dbSNP | Ensembl ].		VAR_056148
	Natural variant	1264	1	R → W. Corresponds to variant rs11244275 [ dbSNP | Ensembl ].		VAR_056149
Experimental info
	Sequence conflict	957	1	F → S in AAD36991. Ref.1
	Sequence conflict	979	1	E → Y in AAD36991. Ref.1
	Sequence conflict	999	1	D → Y in AAD36991. Ref.1
	Sequence conflict	1024	1	A → T in AAD36991. Ref.1
	Sequence conflict	1157	1	T → I in AAD36991. Ref.1
	Sequence conflict	1309	1	K → KARSRLTATSASQ in CAH69983. Ref.2
	Sequence conflict	1309	1	K → MARSRLTATFASQ in AAD36991. Ref.1
	Sequence conflict	1313	1	E → G in AAD36991. Ref.1
	Sequence conflict	1433	1	T → M in BAD92124. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6N6 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: D09DAFB3A900E1BD	FASTA	1,575	171,227
	10 20 30 40 50 60 MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA SHTCGSPPED 70 80 90 100 110 120 FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES TWWQSPSMAF GVQYPTSVNI 130 140 150 160 170 180 TLRLGKAYEI TYVRLKFHTS RPESFAIYKR SRADGPWEPY QFYSASCQKT YGRPEGQYLR 190 200 210 220 230 240 PGEDERVAFC TSEFSDISPL SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR 250 260 270 280 290 300 LNTFGDDIFK DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD 310 320 330 340 350 360 CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG RCHHCRDHTA 370 380 390 400 410 420 GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT CACKPTVTGW KCDRCLPGFH 430 440 450 460 470 480 SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC 490 500 510 520 530 540 FCYGHSKVCA STAQFQVHHI LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL 550 560 570 580 590 600 TAPEKFLGDQ RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP 610 620 630 640 650 660 REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF LTEVRLTSAR 670 680 690 700 710 720 PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP YASCVPCTCN QHGTCDPNTG 730 740 750 760 770 780 ICVCSHHTEG PSCERCLPGF YGNPFAGQAD DCQPCPCPGQ SACTTIPESR EVVCTHCPPG 790 800 810 820 830 840 QRGRRCEVCD DGFFGDPLGL FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG 850 860 870 880 890 900 DHCEHCQEGF YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR 910 920 930 940 950 960 CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC QLGFFGFSIK 970 980 990 1000 1010 1020 GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN FFLTADGTHC QQCPSCYALV 1030 1040 1050 1060 1070 1080 KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL DILLGEAPRG DVYQGHHLLP GAREAFLEQM 1090 1100 1110 1120 1130 1140 MSLEGAVKAA REQLQRLNKG ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE 1150 1160 1170 1180 1190 1200 IPQEGPSQPT KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA 1210 1220 1230 1240 1250 1260 LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL ALLASPGALP 1270 1280 1290 1300 1310 1320 QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT LRQTEPLTKL HQEARAALTQ 1330 1340 1350 1360 1370 1380 ASSSVQAATV TVMGARTLLA DLEGMKLQFP RPKDQAALQR KADSVSDRLL ADTRKKTKQA 1390 1400 1410 1420 1430 1440 ERMLGNAAPL SSSAKKKGRE AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA 1450 1460 1470 1480 1490 1500 SQQVLASEAR RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA 1510 1520 1530 1540 1550 1560 PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL AEIRADKQNL 1570 EAILHSLPEN CASWQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain." Koch M., Olson P.F., Albus A., Jin W., Hunter D.D., Brunken W.J., Burgeson R.E., Champliaud M.-F. J. Cell Biol. 145:605-618(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-522; GLY-544; GLY-770 AND GLY-1082. Tissue: Placenta.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Homo sapiens protein coding cDNA." Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1575, VARIANTS GLY-544; GLY-770 AND GLY-1082. Tissue: Spleen.
[4]	"Recessive LAMC3 mutations cause malformations of occipital cortical development." Barak T., Kwan K.Y., Louvi A., Demirbilek V., Saygi S., Tuysuz B., Choi M., Boyaci H., Doerschner K., Zhu Y., Kaymakcalan H., Yilmaz S., Bakircioglu M., Caglayan A.O., Ozturk A.K., Yasuno K., Brunken W.J., Atalar E. , Yalcinkaya C., Dincer A., Bronen R.A., Mane S., Ozcelik T., Lifton R.P., Sestan N., Bilguvar K., Gunel M. Nat. Genet. 43:590-594(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OCCM ARG-350.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF041835 mRNA. Translation: AAD36991.1. Frameshift. AL583807, AL355872 Genomic DNA. Translation: CAH69983.1. AL583807, AL355872 Genomic DNA. Translation: CAH69984.3. AL355872, AL583807 Genomic DNA. Translation: CAX14981.1. AB208887 mRNA. Translation: BAD92124.1.
IPI	IPI00914899.
RefSeq	NP_006050.3. NM_006059.3.
UniGene	Hs.201805.
3D structure databases
ProteinModelPortal	Q9Y6N6.
SMR	Q9Y6N6. Positions 25-470, 662-996.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y6N6. 20 interactions.
MINT	MINT-7034525.
STRING	9606.ENSP00000354360.
Polymorphism databases
DMDM	308153586.
Proteomic databases
PaxDb	Q9Y6N6.
PRIDE	Q9Y6N6.
Protocols and materials databases
DNASU	10319.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361069; ENSP00000354360; ENSG00000050555.
GeneID	10319.
KEGG	hsa:10319.
UCSC	uc004caa.1. human.
Organism-specific databases
CTD	10319.
GeneCards	GC09P133884.
H-InvDB	HIX0008477.
HGNC	HGNC:6494. LAMC3.
MIM	604349. gene. 614115. phenotype.
neXtProt	NX_Q9Y6N6.
Orphanet	280640. Occipital pachygyria and polymicrogyria.
PharmGKB	PA30282.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG235720.
HOGENOM	HOG000019301.
HOVERGEN	HBG100808.
KO	K06247.
OrthoDB	EOG498TZW.
Enzyme and pathway databases
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling. amb2_neutrophils_pathway. amb2 Integrin signaling.
Gene expression databases
Bgee	Q9Y6N6.
CleanEx	HS_LAMC3.
Genevestigator	Q9Y6N6.
GermOnline	ENSG00000050555. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.260. 1 hit.
InterPro	IPR002049. EGF_laminin. IPR008979. Galactose-bd-like. IPR000034. Laminin_B_type_IV. IPR008211. Laminin_N. [Graphical view]
Pfam	PF00052. Laminin_B. 1 hit. PF00053. Laminin_EGF. 11 hits. PF00055. Laminin_N. 1 hit. [Graphical view]
SMART	SM00180. EGF_Lam. 10 hits. SM00136. LamNT. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. 7 hits. PS01186. EGF_2. 2 hits. PS01248. EGF_LAM_1. 10 hits. PS50027. EGF_LAM_2. 10 hits. PS51115. LAMININ_IVA. 1 hit. PS51117. LAMININ_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LAMC3. human.
GenomeRNAi	10319.
NextBio	39119.
SOURCE	Search...

Entry information

Entry name

LAMC3_HUMAN

Accession

Primary (citable) accession number: Q9Y6N6
Secondary accession number(s): B1APX9, B1APY0, Q59H72

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	October 5, 2010
Last modified:	May 29, 2013
This is version 117 of the entry and version 3 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.