ID A0A2Y9N5P8_DELLE Unreviewed; 1504 AA.
AC A0A2Y9N5P8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Neurexin-1 {ECO:0000256|ARBA:ARBA00044151};
DE AltName: Full=Neurexin I-alpha {ECO:0000256|ARBA:ARBA00044347};
DE AltName: Full=Neurexin-1-alpha {ECO:0000256|ARBA:ARBA00044281};
GN Name=NRXN1 {ECO:0000313|RefSeq:XP_022429570.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022429570.1};
RN [1] {ECO:0000313|RefSeq:XP_022429570.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022429570.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00035005}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00035005}.
CC -!- SIMILARITY: Belongs to the neurexin family.
CC {ECO:0000256|ARBA:ARBA00010241}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_022429570.1; XM_022573862.2.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 6.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF51; NEUREXIN-1; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023207};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00023207};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1504
FT /note="Neurexin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015943832"
FT TRANSMEM 1430..1450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..217
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 219..256
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 283..473
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 480..672
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 676..713
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 718..891
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 905..1080
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1083..1120
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1126..1324
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 201..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1504 AA; 165179 MW; 5780608C53257AA1 CRC64;
MGTALLQRGG CFLVCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR
RQFRNTTLFI DQVEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
KGWIRDVRVN SSQALLVDSG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP
IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG
KFNDNAWHDV KVTRNLRQHS GIGHAMVTIS VDGILTTTGY TQEDYTMLGS DDFFYVGGSP
STADLPGSPV SNNFMGCLKE VVYKNNDVRL ELSRLAKQGD PKMKIHGVVA FKCENVATLD
PITFETPESF VSLPKWNAKK TGSISFDFRT TEPNGLILFS HGKPRHQKDA KHPQMIKVDF
FAIEMLDGHL YLLLDMGSGT IKIKALQKKV NDGEWYHVDF QRDGRSGTIS VNTLRTPYTA
PGESEILDLD DELYLGGLPE NKAGLVFPTE VWTALLNYGY VGCVRDLFID GQSKDIRQMA
EVQSTAGVKP SCSRETAKPC LSNPCKNSGM CRDGWNRYVC DCSGTGYLGR SCEREATVLS
YDGSMFMKIQ LPLVMHTEAE DVSLRFRSQR AYGILMATTS RDSADTLRLE LDAGRVKLTV
NLDCIRINCN SSKGPETLFA GYNLNDNEWH TVRVVRRGKS LKLTVDDQQA MTGQMAGDHT
RLEFHNIETG IITERRYLSS VPSNFIGHLQ SLTFNGMAYI DLCKNGDIDY CELNARFGFR
NIIADPVTFK TKSSYVALAT LQAYTSMHLF FQFKTTSLDG LILYNSGDGN DFIVVELVKG
YLHYVFDLGN GANLIKGSSN KPLNDNQWHN VMISRDTSNL HTVKIDTKIT TQITAGARNL
DLKSDLYIGG VAKETYKSLP KLVHAKEGFQ GCLASVDLNG RLPDLISDAL FCNGQIERGC
EGPSTTCQED SCSNQGVCLQ QWDGFSCDCS MTSFSGPLCN DPGTTYIFSK GGGQITYKWP
PNDRPSTRAD RLAIGFSTVQ KEAVLVRVDS SSGLGDYLEL HIHQGKIGVK FNVGTDDIAI
EESNAIINDG KYHVVRFTRS GGNATLQVDS WPVIERYPAG NNDNERLAIA RQRIPYRLGR
VVDEWLLDKG RQLTIFNSQA TIIIGGKEQG QPFQGQLSGL YYNGLKVLNM AAENDANIAI
VGNVRLVGEV PSSMTTESTA TAMQSEMSTS IMETTTTLAT STARRGKPPT KEPISQTTDD
ILVASAECPS DDEDIDPCEP SSANPTRAGG REPYPGSAEV IRESSSTTGM VVGIVAAAAL
CILILLYAMY KYRNRDEGSY HVDESRNYIS NSAQSNGAVV KEKQPSSAKS ANKNKKNKDK
EYYV
//
