Primary Information | |
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BoMiProt ID | Bomi7435 |
Protein Name | Neurexin-1 |
Organism | Bos taurus |
Uniprot ID | Q28146 |
Milk Fraction | Whey |
Ref Sequence ID | NP_776829.1 |
Aminoacid Length | 1530 |
Molecular Weight | 167939 |
FASTA Sequence | Download |
Gene Name | NRXN1 |
Gene ID | 281950 |
Protein Existence Status | reviewed |
Secondary Information | |
Protein Function | synaptogenesis and cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission.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. |
Biochemical Properties | The extracellular sequences of α‐neurexins contain six LNS domains (LNS1–LNS6) interspersed with epidermal growth factor‐like domains (EGFA–EGFC), followed by a cysteine loop and a highly glycosylated stalk region.These are embedded in the membrane by a single transmembrane region followed by a short (~55 residue) cytoplasmic tail. Alternative splicing of neurexins regulates the interactions of neurexins with a multitude of ligands, including neurexophilins (Nxphs), neuroligins (Nlgns), LRRTMs, cerebellins, and dystroglycan.N‐linked glycans at amino acid positions N146, N156, and N162. |
PTMs | N-glycosylated.O-glycosylated. |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|Q28146|NRX1A_BOVIN Neurexin-1 OS=Bos taurus OX=9913 GN=NRXN1 PE=1 SV=1 MGTALLQRGGCFLLCLSLLLLGCWAELGSGLEFPGAEGQWTRFPKWNACCESEMSFQLKT RSARGLVLYFDDEGFCDFLELILTRGGRLQLSFSIFCAEPATLLTDTPVNDGAWHNVRIR RQFRN*125TTLFIDQVEAKWVEVKSKRRDMTVFSGLFVGGLPPELRAAALKLTLASVREREPF KGWIRDVRVN*190SSLALPVDSGEVKLDDEPPNSGGGSPCEAGEEGEGGVCLNGGVCSVVDDQ AVCDCSRTGFRGKDCSQEDNNVEGLAHLMMGDQGKSKEDNNVEGLAHLMMGDQGKEEYIA TFKGSEYFCYDLSQNPIQSSSDEITLSFKTLQRNGLMLHTGKSADYVNLALKNGAVSLVI NLGSGAFEALVEPVNGKFNDNAWHDVKVTRNLRQTSGIGHAMVNKLHCSVTISVDGILTT TGYTQEDYTMLGSDDFFYVGGSPSTADLPGSPVSNNFMGCLKEVVYKNNDVRLELSRLAK QGDPKMKIHGVVAFKCENVATLDPITFETPESFISLPKWNAKKTGSISFDFRTTEPNGLI LFSHGKPRHQKDAKHPQMIKVDFFAIEMLDGHLYLLLDMGSGTIKIKALQKKVNDGEWYH VDFQRDGRSGTISVNTLRTPYTAPGESQILDLDDELYLGGLPENKAGLVFPTEVWTALLN YGYVGCIRDLFIDGQSKDIRQMAEVQSTAGVKPSCSRETAKPCLS*705NPCKNNGMCRDGWNR YVCDCSGTGYLGRSCEREATVLSYDGSMFMKIQLPVVMHTEAEDVSLRFRSQRAYGILMA TTSRDSADTLRLELDAGRVKLTVNLDCIRINCN*813SSKGPETLFAGYNLNDNEWHTVRVVRR GKSLKLTVDDQQAMTGQMAGDHTRLEFHNIETGIITERRYLSSVPSNFIGHLQSLTFNGM AYIDLCKNGDIDYCELNARFGFRNIIADPVTFKTKSSYVALATLQAYTSMHLFFQFKTTS LDGLILYNSGDGNDFIVVELVKGYLHYVFDLGNGANLIKGSSNKPLNDNQWHNVMISRDT SNLHTVKIDTKITTQITAGARNLDLKSDLYIGGVAKETYKSLPKLVHAKEGFQGCLASVD LNGRLPDLISDALFCNGQIERGCEGPSTTCQEDSCSNQGVCLQQWDGISCDCSMTSFSGP LCNDPGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDY LELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGN*1246ATLQVDSWPVIERY PAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIIIGGKEQGQPFQGQL SGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTT LATSTARRGKPPTKEPVSQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRAGGREPY PGSAEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQ SNGAVVKEKQPSSAKSANKNKKNKDKEYYV |
CATH | Matched CATH superfamily 2.10.25.10 2.60.120.20 2.60.120.200 |
Predicted Disorder Regions | 2 disordered segments; 212nd residue,(1357-1445), (1494-1520) |
DisProt Annotation | |
TM Helix Prediction | 1TMH; (1454-1476) |
PDB ID | 2H0B,2R16,3ASI,3POY,3QCW,3R05,6CW1, |
Additional Comments | In Drosophila case study,Neurexin-1 null mutants are viable and fertile, but have shortened lifespan.Neurexin-1 null mutants exhibit associative learning defect in larvae. |
Bibliography | 1.Wilson, S. C., White, K. I., Zhou, Q., Pfuetzner, R. A., Choi, U. B., Südhof, T. C., & Brunger, A. T. (2019). Structures of neurexophilin-neurexin complexes reveal a regulatory mechanism of alternative splicing. The EMBO journal, 38(22), e101603. https://doi.org/10.15252/embj.2019101603 2.Trotter JH, Hao J, Maxeiner S, Tsetsenis T, Liu Z, Zhuang X, Südhof TC. Synaptic neurexin-1 assembles into dynamically regulated active zone nanoclusters. J Cell Biol. 2019 Aug 5;218(8):2677-2698. doi: 10.1083/jcb.201812076. Epub 2019 Jul 1. PMID: 31262725; PMCID: PMC6683742. |