ID A0A2Y9S7B6_PHYMC Unreviewed; 1514 AA.
AC A0A2Y9S7B6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_023974526.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023974526.1};
RN [1] {ECO:0000313|RefSeq:XP_023974526.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023974526.1};
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_023974526.1; XM_024118758.1.
DR Proteomes; UP000248484; Chromosome 12.
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:UP000248484};
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..1514
FT /note="Neurexin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015905915"
FT TRANSMEM 1440..1460
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..480
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 487..679
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 683..720
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 725..898
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 912..1087
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1090..1127
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1133..1331
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 197..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1514 AA; 166209 MW; BA1E0A8B1C1B501A CRC64;
MGTALLQRGG CFLVCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR
RQFRNTTLFI DQVEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
KGWIRDVRVN SSQALPVDSG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ
AVCDCSRTGF RGKDCSQEDN HVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP
IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG
KFNDNAWHDV KVTRNLRQHS GIGHAMVNKL HCSVTISVDG ILTTTGYTQE DYTMLGSDDF
FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDVRLELS RLAKQGDPKM KIHGVVAFKC
ENVATLDPIT FETPESFVSL PKWNAKKTGS ISFDFRTTEP NGLILFSHGK PRHQKDAKHP
QMIKVDFFAI EMLDGHLYLL LDMGSGTIKI KALQKKVNDG EWYHVDFQRD GRSGTISVNT
LRTPYTAPGE SEILDLDDEL YLGGLPENKA GLVFPTEVWT ALLNYGYVGC IRDLFIDGQS
KDIRQMAEVQ STAGVKPSCS RETAKPCLSN PCKNSGMCRD GWNRYVCDCS GTGYLGRSCE
REATVLSYDG SMFMKIQLPL VMHTEAEDVS LRFRSQRAYG ILMATTSRDS ADTLRLELDA
GRVKLTVNLD CIRINCNSSK GPETLFAGYN LNDNEWHTVR VVRRGKSLKL TVDDQQAMTG
QMAGDHTRLE FHNIETGIIT ERRYLSSVPS NFIGHLQSLT FNGMAYIDLC KNGDIDYCEL
NARFGFRNII ADPVTFKTKS SYVALATLQA YTSMHLFFQF KTTSLDGLIL YNSGDGNDFI
VVELVKGYLH YVFDLGNGAN LIKGSSNKPL NDNQWHNVMI SRDTSNLHTV KIDTKITTQI
TAGARNLDLK SDLYIGGVAK ETYKSLPKLV HAKEGFQGCL ASVDLNGRLP DLISDALFCN
GQIERGCEGP STTCQEDSCS NQGVCLQQWD GFSCDCSMTS FSGPLCNDPG TTYIFSKGGG
QITYKWPPND RPSTRADRLA IGFSTVQKEA VLVRVDSSSG LGDYLELHIH QGKIGVKFNV
GTDDIAIEES NAIINDGKYH VVRFTRSGGN ATLQVDSWPV IERYPAGNND NERLAIARQR
IPYRLGRVVD EWLLDKGRQL TIFNSQATII IGGKEQGQPF QGQLSGLYYN GLKVLNMAAE
NDANIAIVGN VRLVGEVPSS MTTESTATAM QSEMSTSIME TTTTLATSTA RRGKPPTKEP
ISQTTDDILV ASAECPSDDE DIDPCEPSSG GLANPTRAGG REPYPGSAEV IRESSSTTGM
VVGIVAAAAL CILILLYAMY KYRNRDEGSY HVDESRNYIS NSAQSNGAVV KEKQPSSAKS
ANKNKKNKDK EYYV
//
