Q8N2Q7 (NLGN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuroligin-1

Gene names

Name:	NLGN1
Synonyms:	KIAA1070

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	840 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	Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses By similarity.
Subunit structure	Interacts with NRXN1, NRXN2 and NRXN3. Interacts with NLGN3. Interacts with AIP1 and PDZRN3 By similarity. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with GOPC. Ref.5 Ref.6
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Cell junction › synapse By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Note: Enriched in synaptic plasma membranes and clustered in synaptic clefts and postsynaptic densities. Detected at dendritic spines. Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1 By similarity.
Tissue specificity	Expressed in the blood vessel walls (at protein level). Detected in brain, and at lower levels in pancreas islet beta cells. Ref.7 Ref.8
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.
Sequence caution	The sequence BAA83022.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAC11039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-methyl-D-aspartate receptor clustering Inferred from electronic annotation. Source: Compara alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor clustering Inferred from sequence or structural similarity. Source: BHF-UCL calcium-dependent cell-cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB cytoskeletal matrix organization at active zone Inferred from sequence or structural similarity. Source: BHF-UCL heterophilic cell-cell adhesion Inferred from sequence or structural similarity. Source: BHF-UCL neurexin clustering Inferred from sequence or structural similarity. Source: BHF-UCL neuron cell-cell adhesion Inferred from sequence or structural similarity. Source: BHF-UCL neuronal signal transduction Traceable author statement PubMed 15797875. Source: BHF-UCL positive regulation of dendritic spine development Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of excitatory postsynaptic membrane potential Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of filopodium assembly Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of intracellular protein kinase cascade Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of ruffle assembly Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synapse assembly Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic transmission, GABAergic Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic transmission, glutamatergic Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic vesicle endocytosis Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic vesicle exocytosis Inferred from sequence or structural similarity. Source: BHF-UCL postsynaptic density protein 95 clustering Inferred from sequence or structural similarity. Source: BHF-UCL postsynaptic membrane assembly Inferred from sequence or structural similarity. Source: BHF-UCL presynaptic membrane assembly Inferred from sequence or structural similarity. Source: BHF-UCL protein heterotetramerization Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from sequence or structural similarity. Source: BHF-UCL protein targeting Inferred from sequence or structural similarity. Source: UniProtKB receptor localization to synapse Inferred from sequence or structural similarity. Source: BHF-UCL regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL regulation of respiratory gaseous exchange by neurological system process Inferred from electronic annotation. Source: Compara synaptic vesicle clustering Inferred from sequence or structural similarity. Source: BHF-UCL synaptic vesicle targeting Inferred from sequence or structural similarity. Source: UniProtKB terminal button organization Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	N-methyl-D-aspartate selective glutamate receptor complex Inferred from electronic annotation. Source: Compara cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from sequence or structural similarity. Source: BHF-UCL filopodium tip Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic density Traceable author statement PubMed 15797875. Source: BHF-UCL postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cell adhesion molecule binding Inferred from sequence or structural similarity. Source: BHF-UCL neurexin family protein binding Inferred from sequence or structural similarity. Source: UniProtKB protein dimerization activity Inferred from sequence or structural similarity. Source: BHF-UCL receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N2Q7-1)

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.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q8N2Q7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     165-181: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 45	45	Potential
	Chain	46 – 840	795	Neuroligin-1		PRO_0000008640
Regions
	Topological domain	46 – 694	649	Extracellular Potential
	Transmembrane	695 – 715	21	Helical; Potential
	Topological domain	716 – 840	125	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	109	1	N-linked (GlcNAc...) (complex) By similarity
	Glycosylation	300	1	N-linked (GlcNAc...) (complex) By similarity
	Glycosylation	340	1	N-linked (GlcNAc...) (complex) By similarity
	Glycosylation	544	1	N-linked (GlcNAc...) By similarity
	Glycosylation	680	1	O-linked (GalNAc...) By similarity
	Glycosylation	683	1	O-linked (GalNAc...) By similarity
	Disulfide bond	117 ↔ 153		By similarity
	Disulfide bond	339 ↔ 350		By similarity
	Disulfide bond	509 ↔ 543		By similarity
Natural variations
	Alternative sequence	165 – 181	17	Missing in isoform 2.		VSP_007527
Experimental info
	Sequence conflict	711	1	F → L in BAC11039. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 23, 2003. Version 2. Checksum: A3FB21716F62DE29	FASTA	840	93,835
	10 20 30 40 50 60 MALPRCTWPN YVWRAVMACL VHRGLGAPLT LCMLGCLLQA GHVLSQKLDD VDPLVATNFG 70 80 90 100 110 120 KIRGIKKELN NEILGPVIQF LGVPYAAPPT GERRFQPPEP PSPWSDIRNA TQFAPVCPQN 130 140 150 160 170 180 IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDGPLTKK RDEATLNPPD 190 200 210 220 230 240 TDIRDSGGPK PVMVYIHGGS YMEGTGNLYD GSVLASYGNV IVITVNYRLG VLGFLSTGDQ 250 260 270 280 290 300 AAKGNYGLLD LIQALRWTSE NIGFFGGDPL RITVFGSGAG GSCVNLLTLS HYSEGNRWSN 310 320 330 340 350 360 STKGLFQRAI AQSGTALSSW AVSFQPAKYA RMLATKVGCN VSDTVELVEC LQKKPYKELV 370 380 390 400 410 420 DQDIQPARYH IAFGPVIDGD VIPDDPQILM EQGEFLNYDI MLGVNQGEGL KFVENIVDSD 430 440 450 460 470 480 DGISASDFDF AVSNFVDNLY GYPEGKDVLR ETIKFMYTDW ADRHNPETRR KTLLALFTDH 490 500 510 520 530 540 QWVAPAVATA DLHSNFGSPT YFYAFYHHCQ TDQVPAWADA AHGDEVPYVL GIPMIGPTEL 550 560 570 580 590 600 FPCNFSKNDV MLSAVVMTYW TNFAKTGDPN QPVPQDTKFI HTKPNRFEEV AWTRYSQKDQ 610 620 630 640 650 660 LYLHIGLKPR VKEHYRANKV NLWLELVPHL HNLNDISQYT STTTKVPSTD ITFRPTRKNS 670 680 690 700 710 720 VPVTSAFPTA KQDDPKQQPS PFSVDQRDYS TELSVTIAVG ASLLFLNILA FAALYYKKDK 730 740 750 760 770 780 RRHDVHRRCS PQRTTTNDLT HAQEEEIMSL QMKHTDLDHE CESIHPHEVV LRTACPPDYT 790 800 810 820 830 840 LAMRRSPDDV PLMTPNTITM IPNTIPGIQP LHTFNTFTGG QNNTLPHPHP HPHSHSTTRV
	Isoform 2 [UniParc]. Checksum: EA93E8F9801CB8A8	FASTA	823	92,000
	10 20 30 40 50 60 MALPRCTWPN YVWRAVMACL VHRGLGAPLT LCMLGCLLQA GHVLSQKLDD VDPLVATNFG 70 80 90 100 110 120 KIRGIKKELN NEILGPVIQF LGVPYAAPPT GERRFQPPEP PSPWSDIRNA TQFAPVCPQN 130 140 150 160 170 180 IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDDIRDSG GPKPVMVYIH 190 200 210 220 230 240 GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST GDQAAKGNYG LLDLIQALRW 250 260 270 280 290 300 TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR WSNSTKGLFQ RAIAQSGTAL 310 320 330 340 350 360 SSWAVSFQPA KYARMLATKV GCNVSDTVEL VECLQKKPYK ELVDQDIQPA RYHIAFGPVI 370 380 390 400 410 420 DGDVIPDDPQ ILMEQGEFLN YDIMLGVNQG EGLKFVENIV DSDDGISASD FDFAVSNFVD 430 440 450 460 470 480 NLYGYPEGKD VLRETIKFMY TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG 490 500 510 520 530 540 SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP TELFPCNFSK NDVMLSAVVM 550 560 570 580 590 600 TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ KDQLYLHIGL KPRVKEHYRA 610 620 630 640 650 660 NKVNLWLELV PHLHNLNDIS QYTSTTTKVP STDITFRPTR KNSVPVTSAF PTAKQDDPKQ 670 680 690 700 710 720 QPSPFSVDQR DYSTELSVTI AVGASLLFLN ILAFAALYYK KDKRRHDVHR RCSPQRTTTN 730 740 750 760 770 780 DLTHAQEEEI MSLQMKHTDL DHECESIHPH EVVLRTACPP DYTLAMRRSP DDVPLMTPNT 790 800 810 820 ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST TRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[2]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Duodenum.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-823. Tissue: Embryo.
[5]	"Binding of neuroligins to PSD-95." Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K., Takai Y., Rosahl T.W., Suedhof T.C. Science 277:1511-1515(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DLG4.
[6]	"Solution structure of GOPC PDZ domain and its interaction with the C-terminal motif of neuroligin." Li X., Zhang J., Cao Z., Wu J., Shi Y. Protein Sci. 15:2149-2158(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GOPC.
[7]	"Expression of neurexin, neuroligin, and their cytoplasmic binding partners in the pancreatic beta-cells and the involvement of neuroligin in insulin secretion." Suckow A.T., Comoletti D., Waldrop M.A., Mosedale M., Egodage S., Taylor P., Chessler S.D. Endocrinology 149:6006-6017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[8]	"The synaptic proteins neurexins and neuroligins are widely expressed in the vascular system and contribute to its functions." Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B., Cera M.R., Mascia L., Bussolino F., Arese M. Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB028993 mRNA. Translation: BAA83022.2. Different initiation. AC008082 Genomic DNA. No translation available. AC008120 Genomic DNA. No translation available. AC092923 Genomic DNA. No translation available. AC092967 Genomic DNA. No translation available. AC110871 Genomic DNA. No translation available. AC131158 Genomic DNA. No translation available. BC032555 mRNA. Translation: AAH32555.1. AK074522 mRNA. Translation: BAC11039.1. Different initiation.
IPI	IPI00903001. IPI00927327.
RefSeq	NP_055747.1. NM_014932.2.
UniGene	Hs.478289.
3D structure databases
ProteinModelPortal	Q8N2Q7.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1901478.
STRING	9606.ENSP00000354541.
Protein family/group databases
MEROPS	S09.994.
PTM databases
PhosphoSite	Q8N2Q7.
Polymorphism databases
DMDM	31076822.
Proteomic databases
PaxDb	Q8N2Q7.
PRIDE	Q8N2Q7.
Protocols and materials databases
DNASU	22871.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361589; ENSP00000354541; ENSG00000169760. ENST00000457714; ENSP00000392500; ENSG00000169760. ENST00000545397; ENSP00000441108; ENSG00000169760.
GeneID	22871.
KEGG	hsa:22871.
UCSC	uc003fio.1. human.
Organism-specific databases
CTD	22871.
GeneCards	GC03P173114.
HGNC	HGNC:14291. NLGN1.
HPA	HPA006680.
MIM	600568. gene.
neXtProt	NX_Q8N2Q7.
PharmGKB	PA31647.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2272.
HOGENOM	HOG000231424.
HOVERGEN	HBG008839.
InParanoid	Q8N2Q7.
KO	K07378.
OrthoDB	EOG4CZBF6.
Gene expression databases
ArrayExpress	Q8N2Q7.
Bgee	Q8N2Q7.
CleanEx	HS_NLGN1.
Genevestigator	Q8N2Q7.
GermOnline	ENSG00000169760. Homo sapiens.
Family and domain databases
InterPro	IPR002018. CarbesteraseB. IPR019819. Carboxylesterase_B_CS. IPR000460. Neuroligin. [Graphical view]
Pfam	PF00135. COesterase. 1 hit. [Graphical view]
PRINTS	PR01090. NEUROLIGIN.
PROSITE	PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NLGN1. human.
GenomeRNAi	22871.
NextBio	43403.
SOURCE	Search...

Entry information

Entry name

NLGN1_HUMAN

Accession

Primary (citable) accession number: Q8N2Q7
Secondary accession number(s): Q9UPT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 23, 2003
Last modified:	May 1, 2013
This is version 105 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.