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Protein

Neurexin-1

Gene

NRXN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca2+-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca2+-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi345 – 3451Calcium 11 Publication
Metal bindingi362 – 3621Calcium 1; via carbonyl oxygen1 Publication
Metal bindingi430 – 4301Calcium 1; via carbonyl oxygen1 Publication
Metal bindingi788 – 7881Calcium 21 Publication
Metal bindingi805 – 8051Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi864 – 8641Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi1199 – 11991Calcium 3By similarity
Metal bindingi1216 – 12161Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1298 – 12981Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1300 – 13001Calcium 3By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • neuroligin family protein binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neurexin-1
Alternative name(s):
Neurexin I-alpha
Neurexin-1-alpha
Gene namesi
Name:NRXN1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 14541424ExtracellularSequence analysisAdd
BLAST
Transmembranei1455 – 147521HelicalSequence analysisAdd
BLAST
Topological domaini1476 – 153055CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030By similarityAdd
BLAST
Chaini31 – 15301500Neurexin-1PRO_0000019489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence analysis
Disulfide bondi228 ↔ 243By similarity
Disulfide bondi245 ↔ 255By similarity
Disulfide bondi460 ↔ 496
Disulfide bondi666 ↔ 695
Disulfide bondi703 ↔ 714
Glycosylationi705 – 7051O-linked (Glc...)1 Publication
Disulfide bondi708 ↔ 723
Disulfide bondi725 ↔ 735
Glycosylationi813 – 8131N-linked (GlcNAc...)Sequence analysis
Disulfide bondi906 ↔ 914
Disulfide bondi1075 ↔ 1103
Disulfide bondi1110 ↔ 1121
Disulfide bondi1115 ↔ 1130
Disulfide bondi1132 ↔ 1142
Glycosylationi1246 – 12461N-linked (GlcNAc...)3 Publications

Post-translational modificationi

N-glycosylated.
O-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ28146.

Interactioni

Subunit structurei

Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer interacts with one NRXN1 dimer. Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1, NLGN2, NLGN3 and NLGN4; these interactions are calcium-dependent. Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 (By similarity). Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 (By similarity). Alpha-type isoforms (neurexin-1-alpha) interact (via laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via alpha-dystroglycan chain). Alpha-type isoforms interact with alpha-latrotoxin from spider venom. The cytoplasmic C-terminal region binds to CASK, CASKIN1 and APBA1. Interacts with SYT13 and SYTL1.By similarity5 Publications

GO - Molecular functioni

  • neuroligin family protein binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-59135N.

Structurei

Secondary structure

1
1530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi299 – 31113Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi317 – 33115Combined sources
Beta strandi335 – 3406Combined sources
Beta strandi345 – 3528Combined sources
Beta strandi355 – 36410Combined sources
Beta strandi366 – 3716Combined sources
Beta strandi374 – 3763Combined sources
Beta strandi378 – 3825Combined sources
Beta strandi384 – 3918Combined sources
Beta strandi410 – 4145Combined sources
Turni415 – 4173Combined sources
Beta strandi418 – 4236Combined sources
Beta strandi425 – 4273Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi435 – 4406Combined sources
Helixi445 – 4473Combined sources
Beta strandi448 – 4503Combined sources
Beta strandi458 – 47013Combined sources
Helixi475 – 4817Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi505 – 5073Combined sources
Beta strandi509 – 5113Combined sources
Beta strandi514 – 5163Combined sources
Beta strandi522 – 53211Combined sources
Beta strandi538 – 5447Combined sources
Beta strandi563 – 5697Combined sources
Beta strandi572 – 58110Combined sources
Beta strandi583 – 5886Combined sources
Beta strandi595 – 5973Combined sources
Beta strandi599 – 6068Combined sources
Beta strandi609 – 6146Combined sources
Beta strandi617 – 6226Combined sources
Beta strandi624 – 6263Combined sources
Beta strandi636 – 6405Combined sources
Helixi655 – 6584Combined sources
Beta strandi665 – 6728Combined sources
Beta strandi675 – 6773Combined sources
Helixi679 – 6824Combined sources
Turni684 – 6874Combined sources
Beta strandi691 – 6944Combined sources
Helixi702 – 7043Combined sources
Helixi709 – 7113Combined sources
Beta strandi713 – 7164Combined sources
Beta strandi718 – 7247Combined sources
Turni726 – 7294Combined sources
Beta strandi730 – 7323Combined sources
Beta strandi741 – 7477Combined sources
Beta strandi750 – 77021Combined sources
Beta strandi774 – 7829Combined sources
Beta strandi784 – 7863Combined sources
Beta strandi789 – 7957Combined sources
Beta strandi798 – 8058Combined sources
Beta strandi819 – 8235Combined sources
Beta strandi829 – 8313Combined sources
Beta strandi833 – 8408Combined sources
Beta strandi843 – 8486Combined sources
Beta strandi853 – 8575Combined sources
Beta strandi859 – 8613Combined sources
Beta strandi865 – 87410Combined sources
Beta strandi889 – 8979Combined sources
Helixi902 – 9076Combined sources
Beta strandi914 – 9163Combined sources
Beta strandi919 – 9213Combined sources
Beta strandi930 – 9323Combined sources
Beta strandi934 – 9363Combined sources
Beta strandi938 – 9425Combined sources
Beta strandi950 – 9578Combined sources
Beta strandi963 – 9719Combined sources
Beta strandi975 – 9817Combined sources
Beta strandi984 – 99310Combined sources
Beta strandi995 – 9995Combined sources
Beta strandi1008 – 10103Combined sources
Beta strandi1012 – 10187Combined sources
Beta strandi1023 – 10286Combined sources
Beta strandi1031 – 10366Combined sources
Beta strandi1049 – 10524Combined sources
Helixi1056 – 10616Combined sources
Beta strandi1069 – 10713Combined sources
Beta strandi1074 – 108310Combined sources
Turni1088 – 10914Combined sources
Beta strandi1093 – 110210Combined sources
Beta strandi1114 – 11163Combined sources
Beta strandi1120 – 11234Combined sources
Beta strandi1125 – 11317Combined sources
Turni1133 – 11353Combined sources
Beta strandi1136 – 11394Combined sources
Beta strandi1148 – 116114Combined sources
Helixi1164 – 11663Combined sources
Beta strandi1170 – 118011Combined sources
Beta strandi1184 – 119310Combined sources
Turni1195 – 11973Combined sources
Beta strandi1200 – 12067Combined sources
Beta strandi1209 – 121911Combined sources
Beta strandi1221 – 12244Combined sources
Beta strandi1232 – 12343Combined sources
Beta strandi1236 – 12438Combined sources
Beta strandi1246 – 12516Combined sources
Beta strandi1257 – 12593Combined sources
Beta strandi1302 – 13098Combined sources
Turni1310 – 13134Combined sources
Beta strandi1318 – 13258Combined sources
Helixi1330 – 13356Combined sources
Beta strandi1341 – 135010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0BX-ray2.10A/B/C/D295-491[»]
2R16X-ray1.04A737-925[»]
3ASIX-ray2.30A923-1353[»]
3POYX-ray3.02A296-1349[»]
3QCWX-ray2.65A/B31-805[»]
A/B816-1355[»]
3R05X-ray2.95A/B31-1355[»]
ProteinModelPortaliQ28146.
SMRiQ28146. Positions 295-491, 739-922, 1146-1356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28146.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 212182Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini213 – 25644EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini299 – 496198Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini503 – 695193Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini699 – 73638EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini741 – 914174Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini928 – 1103176Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini1106 – 114338EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini1149 – 1347199Laminin G-like 6PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1377 – 13804Poly-Thr
Compositional biasi1462 – 14654Poly-Ala

Sequence similaritiesi

Belongs to the neurexin family.Curated
Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 6 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000230481.
HOVERGENiHBG052670.
InParanoidiQ28146.

Family and domain databases

Gene3Di2.60.120.200. 6 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR001791. Laminin_G.
IPR029824. Neurexin-1.
IPR003585. Neurexin-like.
IPR027789. Syndecan/Neurexin_dom.
[Graphical view]
PANTHERiPTHR10127:SF565. PTHR10127:SF565. 4 hits.
PfamiPF00008. EGF. 1 hit.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 5 hits.
PF01034. Syndecan. 1 hit.
[Graphical view]
SMARTiSM00294. 4.1m. 1 hit.
SM00181. EGF. 3 hits.
SM00282. LamG. 6 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 7 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS50026. EGF_3. 3 hits.
PS50025. LAM_G_DOMAIN. 6 hits.
[Graphical view]

Sequences (16)i

Sequence statusi: Complete.

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

This entry describes 16 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Note: Two isoform types, alpha-type and beta-type are produced by alternative promoter usage. In addition there are at least five alternatively spliced sites, each of which may be spliced in up to seven different ways. Combinatorial splicing at each of these five sites may lead to the generation of at least 96 isoforms but for simplicity only individual splice events are explicitly described below. Beta-type isoforms share the possibility of alternative splicing at sites 4 and 5. Experimental confirmation may be lacking for some isoforms.2 Publications

Isoform 1a (identifier: Q28146-1) [UniParc]FASTAAdd to basket

Also known as: Alpha-1A2A3A4A5A

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.

« Hide

        10         20         30         40         50
MGTALLQRGG CFLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC
60 70 80 90 100
ESEMSFQLKT RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP
110 120 130 140 150
ATLLTDTPVN DGAWHNVRIR RQFRNTTLFI DQVEAKWVEV KSKRRDMTVF
160 170 180 190 200
SGLFVGGLPP ELRAAALKLT LASVREREPF KGWIRDVRVN SSLALPVDSG
210 220 230 240 250
EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ AVCDCSRTGF
260 270 280 290 300
RGKDCSQEDN NVEGLAHLMM GDQGKSKEDN NVEGLAHLMM GDQGKEEYIA
310 320 330 340 350
TFKGSEYFCY DLSQNPIQSS SDEITLSFKT LQRNGLMLHT GKSADYVNLA
360 370 380 390 400
LKNGAVSLVI NLGSGAFEAL VEPVNGKFND NAWHDVKVTR NLRQTSGIGH
410 420 430 440 450
AMVNKLHCSV TISVDGILTT TGYTQEDYTM LGSDDFFYVG GSPSTADLPG
460 470 480 490 500
SPVSNNFMGC LKEVVYKNND VRLELSRLAK QGDPKMKIHG VVAFKCENVA
510 520 530 540 550
TLDPITFETP ESFISLPKWN AKKTGSISFD FRTTEPNGLI LFSHGKPRHQ
560 570 580 590 600
KDAKHPQMIK VDFFAIEMLD GHLYLLLDMG SGTIKIKALQ KKVNDGEWYH
610 620 630 640 650
VDFQRDGRSG TISVNTLRTP YTAPGESQIL DLDDELYLGG LPENKAGLVF
660 670 680 690 700
PTEVWTALLN YGYVGCIRDL FIDGQSKDIR QMAEVQSTAG VKPSCSRETA
710 720 730 740 750
KPCLSNPCKN NGMCRDGWNR YVCDCSGTGY LGRSCEREAT VLSYDGSMFM
760 770 780 790 800
KIQLPVVMHT EAEDVSLRFR SQRAYGILMA TTSRDSADTL RLELDAGRVK
810 820 830 840 850
LTVNLDCIRI NCNSSKGPET LFAGYNLNDN EWHTVRVVRR GKSLKLTVDD
860 870 880 890 900
QQAMTGQMAG DHTRLEFHNI ETGIITERRY LSSVPSNFIG HLQSLTFNGM
910 920 930 940 950
AYIDLCKNGD IDYCELNARF GFRNIIADPV TFKTKSSYVA LATLQAYTSM
960 970 980 990 1000
HLFFQFKTTS LDGLILYNSG DGNDFIVVEL VKGYLHYVFD LGNGANLIKG
1010 1020 1030 1040 1050
SSNKPLNDNQ WHNVMISRDT SNLHTVKIDT KITTQITAGA RNLDLKSDLY
1060 1070 1080 1090 1100
IGGVAKETYK SLPKLVHAKE GFQGCLASVD LNGRLPDLIS DALFCNGQIE
1110 1120 1130 1140 1150
RGCEGPSTTC QEDSCSNQGV CLQQWDGISC DCSMTSFSGP LCNDPGTTYI
1160 1170 1180 1190 1200
FSKGGGQITY KWPPNDRPST RADRLAIGFS TVQKEAVLVR VDSSSGLGDY
1210 1220 1230 1240 1250
LELHIHQGKI GVKFNVGTDD IAIEESNAII NDGKYHVVRF TRSGGNATLQ
1260 1270 1280 1290 1300
VDSWPVIERY PAGNNDNERL AIARQRIPYR LGRVVDEWLL DKGRQLTIFN
1310 1320 1330 1340 1350
SQATIIIGGK EQGQPFQGQL SGLYYNGLKV LNMAAENDAN IAIVGNVRLV
1360 1370 1380 1390 1400
GEVPSSMTTE STATAMQSEM STSIMETTTT LATSTARRGK PPTKEPVSQT
1410 1420 1430 1440 1450
TDDILVASAE CPSDDEDIDP CEPSSGGLAN PTRAGGREPY PGSAEVIRES
1460 1470 1480 1490 1500
SSTTGMVVGI VAAAALCILI LLYAMYKYRN RDEGSYHVDE SRNYISNSAQ
1510 1520 1530
SNGAVVKEKQ PSSAKSANKN KKNKDKEYYV
Length:1,530
Mass (Da):167,939
Last modified:November 1, 1996 - v1
Checksum:i8A4E4A75C4EC03D1
GO
Isoform 2a (identifier: Q28146-2) [UniParc]FASTAAdd to basket

Also known as: Alpha-1B

The sequence of this isoform differs from the canonical sequence as follows:
     278-293: Missing.

Show »
Length:1,514
Mass (Da):166,184
Checksum:iCD1B8650A183C789
GO
Isoform 3a (identifier: Q28146-3) [UniParc]FASTAAdd to basket

Also known as: Alpha-1C

The sequence of this isoform differs from the canonical sequence as follows:
     258-258: Missing.
     278-293: Missing.

Show »
Length:1,513
Mass (Da):166,055
Checksum:i4BF85979B6828A64
GO
Isoform 4a (identifier: Q28146-4) [UniParc]FASTAAdd to basket

Also known as: Alpha-1D

The sequence of this isoform differs from the canonical sequence as follows:
     274-293: Missing.

Show »
Length:1,510
Mass (Da):165,783
Checksum:i999348A15A299E5B
GO
Isoform 5a (identifier: Q28146-5) [UniParc]FASTAAdd to basket

Also known as: Alpha-1E

The sequence of this isoform differs from the canonical sequence as follows:
     258-258: Missing.
     274-293: Missing.

Show »
Length:1,509
Mass (Da):165,654
Checksum:iDE92054CBD9D8970
GO
Isoform 6a (identifier: Q28146-6) [UniParc]FASTAAdd to basket

Also known as: Alpha-1F

The sequence of this isoform differs from the canonical sequence as follows:
     264-273: Missing.
     278-293: Missing.

Show »
Length:1,504
Mass (Da):165,130
Checksum:i00CF8E297D4306EC
GO
Isoform 7a (identifier: Q28146-7) [UniParc]FASTAAdd to basket

Also known as: Alpha-1G

The sequence of this isoform differs from the canonical sequence as follows:
     258-293: Missing.

Show »
Length:1,494
Mass (Da):164,028
Checksum:i3ACA6902A43B3F36
GO
Isoform 8a (identifier: Q28146-8) [UniParc]FASTAAdd to basket

Also known as: Alpha-2B

The sequence of this isoform differs from the canonical sequence as follows:
     403-409: Missing.

Show »
Length:1,523
Mass (Da):167,157
Checksum:i2A97DE64CF3B1AB8
GO
Isoform 9a (identifier: Q28146-9) [UniParc]FASTAAdd to basket

Also known as: Alpha-2C

The sequence of this isoform differs from the canonical sequence as follows:
     395-409: Missing.

Show »
Length:1,515
Mass (Da):166,402
Checksum:i505A40B67ECA57A8
GO
Isoform 10a (identifier: Q28146-10) [UniParc]FASTAAdd to basket

Also known as: Alpha-3B

The sequence of this isoform differs from the canonical sequence as follows:
     806-815: DCIRINCNSS → G

Show »
Length:1,521
Mass (Da):166,890
Checksum:iB36B0040832AD591
GO
Isoform 11a (identifier: Q28146-11) [UniParc]FASTAAdd to basket

Also known as: Alpha-4B

The sequence of this isoform differs from the canonical sequence as follows:
     1263-1292: Missing.

Show »
Length:1,500
Mass (Da):164,376
Checksum:iFFF0536B1443D542
GO
Isoform 12a (identifier: Q28146-12) [UniParc]FASTAAdd to basket

Also known as: Alpha-5B

The sequence of this isoform differs from the canonical sequence as follows:
     1426-1428: Missing.

Show »
Length:1,527
Mass (Da):167,711
Checksum:i4E97EBE1D1383A03
GO
Isoform 1b (identifier: Q28142-1) [UniParc]FASTAAdd to basket

Also known as: Beta-4A5A

The sequence of this isoform can be found in the external entry Q28142.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:467
Mass (Da):50,084
GO
Isoform 2b (identifier: Q28142-2) [UniParc]FASTAAdd to basket

Also known as: Beta-4A5B

The sequence of this isoform can be found in the external entry Q28142.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:464
Mass (Da):49,857
GO
Isoform 3b (identifier: Q28142-3) [UniParc]FASTAAdd to basket

Also known as: Beta-4B5A

The sequence of this isoform can be found in the external entry Q28142.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:437
Mass (Da):46,521
GO
Isoform 4b (identifier: Q28142-4) [UniParc]FASTAAdd to basket

Also known as: Beta-4B5B

The sequence of this isoform can be found in the external entry Q28142.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:434
Mass (Da):46,294
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei258 – 29336Missing in isoform 7a. CuratedVSP_003475Add
BLAST
Alternative sequencei258 – 2581Missing in isoform 3a and isoform 5a. CuratedVSP_003474
Alternative sequencei264 – 27310Missing in isoform 6a. CuratedVSP_003476
Alternative sequencei274 – 29320Missing in isoform 4a and isoform 5a. CuratedVSP_003477Add
BLAST
Alternative sequencei278 – 29316Missing in isoform 2a, isoform 3a and isoform 6a. CuratedVSP_003478Add
BLAST
Alternative sequencei395 – 40915Missing in isoform 9a. CuratedVSP_003479Add
BLAST
Alternative sequencei403 – 4097Missing in isoform 8a. CuratedVSP_003480
Alternative sequencei806 – 81510DCIRINCNSS → G in isoform 10a. CuratedVSP_003481
Alternative sequencei1263 – 129230Missing in isoform 11a. CuratedVSP_003482Add
BLAST
Alternative sequencei1426 – 14283Missing in isoform 12a. CuratedVSP_003483

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14855 mRNA. Translation: AAA74123.1.
PIRiI45944.
RefSeqiNP_776829.1. NM_174404.2. [Q28146-1]
UniGeneiBt.5497.

Genome annotation databases

GeneIDi281950.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14855 mRNA. Translation: AAA74123.1.
PIRiI45944.
RefSeqiNP_776829.1. NM_174404.2. [Q28146-1]
UniGeneiBt.5497.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0BX-ray2.10A/B/C/D295-491[»]
2R16X-ray1.04A737-925[»]
3ASIX-ray2.30A923-1353[»]
3POYX-ray3.02A296-1349[»]
3QCWX-ray2.65A/B31-805[»]
A/B816-1355[»]
3R05X-ray2.95A/B31-1355[»]
ProteinModelPortaliQ28146.
SMRiQ28146. Positions 295-491, 739-922, 1146-1356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59135N.

Proteomic databases

PRIDEiQ28146.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281950.

Organism-specific databases

CTDi9378.

Phylogenomic databases

HOGENOMiHOG000230481.
HOVERGENiHBG052670.
InParanoidiQ28146.

Miscellaneous databases

EvolutionaryTraceiQ28146.
NextBioi20805826.

Family and domain databases

Gene3Di2.60.120.200. 6 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR001791. Laminin_G.
IPR029824. Neurexin-1.
IPR003585. Neurexin-like.
IPR027789. Syndecan/Neurexin_dom.
[Graphical view]
PANTHERiPTHR10127:SF565. PTHR10127:SF565. 4 hits.
PfamiPF00008. EGF. 1 hit.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 5 hits.
PF01034. Syndecan. 1 hit.
[Graphical view]
SMARTiSM00294. 4.1m. 1 hit.
SM00181. EGF. 3 hits.
SM00282. LamG. 6 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 7 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS50026. EGF_3. 3 hits.
PS50025. LAM_G_DOMAIN. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons."
    Ullrich B., Ushkaryov Y.A., Suedhof T.C.
    Neuron 14:497-507(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Brain.
  2. "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin."
    Ushkaryov Y.A., Petrenko A.G., Geppert M., Suedhof T.C.
    Science 257:50-56(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH ALPHA-LATROTOXIN, TISSUE SPECIFICITY, GLYCOSYLATION.
    Tissue: Brain.
  3. "Structure and evolution of neurexophilin."
    Petrenko A.G., Ullrich B., Missler M., Krasnoperov V., Rosahl T.W., Suedhof T.C.
    J. Neurosci. 16:4360-4369(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NXPH1.
  4. "Crystal structure of the second LNS/LG domain from neurexin 1alpha: Ca2+ binding and the effects of alternative splicing."
    Sheckler L.R., Henry L., Sugita S., Suedhof T.C., Rudenko G.
    J. Biol. Chem. 281:22896-22905(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 295-491, CALCIUM-BINDING.
  5. "Regulation of neurexin 1beta tertiary structure and ligand binding through alternative splicing."
    Shen K.C., Kuczynska D.A., Wu I.J., Murray B.H., Sheckler L.R., Rudenko G.
    Structure 16:422-431(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF 737-925 IN COMPLEX WITH CALCIUM, ALTERNATIVE SPLICING, DISULFIDE BOND.
  6. "Structural basis for variant-specific neuroligin-binding by alpha-neurexin."
    Tanaka H., Nogi T., Yasui N., Iwasaki K., Takagi J.
    PLoS ONE 6:E19411-E19411(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 923-1353, GLYCOSYLATION AT ASN-1246, INTERACTION WITH NLGN1, ELECTRON MICROSCOPY, DISULFIDE BONDS.
  7. "The crystal structure of the alpha-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function."
    Miller M.T., Mileni M., Comoletti D., Stevens R.C., Harel M., Taylor P.
    Structure 19:767-778(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 296-1349, GLYCOSYLATION AT SER-705 AND ASN-1246, INTERACTION WITH NLGN1, DISULFIDE BONDS.
  8. "The structure of neurexin 1alpha reveals features promoting a role as synaptic organizer."
    Chen F., Venugopal V., Murray B., Rudenko G.
    Structure 19:779-789(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 31-1355, GLYCOSYLATION AT ASN-1246, DISULFIDE BONDS.

Entry informationi

Entry nameiNRX1A_BOVIN
AccessioniPrimary (citable) accession number: Q28146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.