8.A.74.1.2
Neurexin-1 (NRX1) of 1477 aas and 2 TMSs, one N-terminal and one C-terminal. It is a cell surface protein involved in
cell-cell-interactions, exocytosis of secretory granules and regulation
of signal transmission including several transport systems. Neurexin function is isoform-specific. It is found in trans-synaptic tripartite
complexes which consist of one unit of the cerebellin-1 (Cbln1) hexamer, four monomeric neurexins containing a
splice site 4 insertion at presynaptic terminals and the postsynaptic GluD2 dimers (Matsuda 2016). The trans-synaptic interaction of postsynaptic glutamate receptor δ2 (GluRδ2, an orthologue of TC#1.A.10.1.8) and presynaptic neurexins through cerebellin precursor protein 1 (Cbln1) mediates synapse formation in vivo in the cerebellum (Lee et al. 2012). Members of the neurexin family appear to be homologous to domains in some members of TC family 9.B.87. Neurexin-1-β (NRX1B; P58400; 472 aas with 2 TMSs, N- and C-terminal) is a neuronal cell surface protein involved in cell recognition and cell
adhesion by forming intracellular junctions through binding to
neuroligins. Plays a role in formation of synaptic junctions. It is a synapse organizer that provides molecular codes for synaptic plasticity (Connor and Siddiqui 2023). Major brain disorders emerge when the functions of these proteins are compromised. There are several families of these organizers that govern synapses. They are diverse, but converge on the structure, function, and plasticity of synapses (Connor and Siddiqui 2023).
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| Accession Number: | Q9ULB1 |
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| Protein Name: | Neurexin-1 |
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| Length: | 1477 |
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| Molecular Weight: | 161883.00 |
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| Species: | Homo sapiens (Human) [9606] |
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| Number of TMSs: | 2 |
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| Location1 / Topology2 / Orientation3: |
Cell membrane1 / Single-pass type I membrane protein2 |
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| Substrate |
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1: MGTALLQRGG CFLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
61: RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR
121: RQFRNTTLFI DQVEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
181: KGWIRDVRVN SSQVLPVDSG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ
241: AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP
301: IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG
361: KFNDNAWHDV KVTRNLRQHS GIGHAMVTIS VDGILTTTGY TQEDYTMLGS DDFFYVGGSP
421: STADLPGSPV SNNFMGCLKE VVYKNNDVRL ELSRLAKQGD PKMKIHGVVA FKCENVATLD
481: PITFETPESF ISLPKWNAKK TGSISFDFRT TEPNGLILFS HGKPRHQKDA KHPQMIKVDF
541: FAIEMLDGHL YLLLDMGSGT IKIKALLKKV NDGEWYHVDF QRDGRSGTIS VNTLRTPYTA
601: PGESEILDLD DELYLGGLPE NKAGLVFPTE VWTALLNYGY VGCIRDLFID GQSKDIRQMA
661: EVQSTAGVKP SCSKETAKPC LSNPCKNNGM CRDGWNRYVC DCSGTGYLGR SCEREATVLS
721: YDGSMFMKIQ LPVVMHTEAE DVSLRFRSQR AYGILMATTS RDSADTLRLE LDAGRVKLTV
781: NLDCIRINCN SSKGPETLFA GYNLNDNEWH TVRVVRRGKS LKLTVDDQQA MTGQMAGDHT
841: RLEFHNIETG IITERRYLSS VPSNFIGHLQ SLTFNGMAYI DLCKNGDIDY CELNARFGFR
901: NIIADPVTFK TKSSYVALAT LQAYTSMHLF FQFKTTSLDG LILYNSGDGN DFIVVELVKG
961: YLHYVFDLGN GANLIKGSSN KPLNDNQWHN VMISRDTSNL HTVKIDTKIT TQITAGARNL
1021: DLKSDLYIGG VAKETYKSLP KLVHAKEGFQ GCLASVDLNG RLPDLISDAL FCNGQIERGC
1081: EGPSTTCQED SCSNQGVCLQ QWDGFSCDCS MTSFSGPLCN DPGTTYIFSK GGGQITYKWP
1141: PNDRPSTRAD RLAIGFSTVQ KEAVLVRVDS SSGLGDYLEL HIHQGKIGVK FNVGTDDIAI
1201: EESNAIINDG KYHVVRFTRS GGNATLQVDS WPVIERYPAG RQLTIFNSQA TIIIGGKEQG
1261: QPFQGQLSGL YYNGLKVLNM AAENDANIAI VGNVRLVGEV PSSMTTESTA TAMQSEMSTS
1321: IMETTTTLAT STARRGKPPT KEPISQTTDD ILVASAECPS DDEDIDPCEP SSGGLANPTR
1381: AGGREPYPGS AEVIRESSST TGMVVGIVAA AALCILILLY AMYKYRNRDE GSYHVDESRN
1441: YISNSAQSNG AVVKEKQPSS AKSSNKNKKN KDKEYYV