ID A0A452CMN2_BALAS Unreviewed; 1470 AA.
AC A0A452CMN2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Neurexin-1 isoform X16 {ECO:0000313|RefSeq:XP_028024274.1};
GN Name=NRXN1 {ECO:0000313|RefSeq:XP_028024274.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028024274.1};
RN [1] {ECO:0000313|RefSeq:XP_028024274.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028024274.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC Presynaptic cell membrane {ECO:0000256|ARBA:ARBA00035005}; Single-pass
CC type I membrane protein {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_028024274.1; XM_028168473.1.
DR Proteomes; UP000261681; 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 InterPro; IPR027789; Syndecan/Neurexin_dom.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR Pfam; PF01034; Syndecan; 1.
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:ARBA00022974};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
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..1470
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019485515"
FT TRANSMEM 1396..1416
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 263..445
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 452..644
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 648..685
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 690..854
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 868..1043
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1046..1083
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1089..1287
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 198..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1470 AA; 161422 MW; C481B8B87C70BB11 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 RGKDCSQGKE EYIATFKGSE YFCYDLSQNP IQSSSDEITL SFKTLQRNGL
MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG KFNDNAWHDV KVTRNLRQVT
ISVDGILTTT GYTQEDYTML GSDDFFYVGG SPSTADLPGS PVSNNFMGCL KEVVYKNNDV
RLELSRLAKQ GDPKMKIHGV VAFKCENVAT LDPITFETPE SFISLPKWNA KKTGSISFDF
RTTEPNGLIL FSHGKPRHQK DAKHPQMIKV DFFAIEMLDG HLYLLLDMGS GTIKIKALQK
KVNDGEWYHV DFQRDGRSGT ISVNTLRTPY TAPGESEILD LDDELYLGGL PENKAGLVFP
TEVWTALLNY GYVGCIRDLF IDGQSKDIRQ MAEVQSTAGV KPSCSRETAK PCLSNPCKNS
GMCRDGWNRY VCDCSGTGYL GRSCEREATV LSYDGSMFMK IQLPLVMHTE AEDVSLRFRS
QRAYGILMAT TSRDSADTLR LELDAGRVKL TVNLGKGPET LFAGYNLNDN EWHTVRVVRR
GKSLKLTVDD QQAMTGQMAG DHTRLEFHNI ETGIITERRY LSSVPSNFIG HLQSLTFNGM
AYIDLCKNGD IDYCELNARF GFRNIIADPV TFKTKSSYVA LATLQAYTSM HLFFQFKTTS
LDGLILYNSG DGNDFIVVEL VKGYLHYVFD LGNGANLIKG SSNKPLNDNQ WHNVMISRDT
SNLHTVKIDT KITTQITAGA RNLDLKSDLY IGGVAKETYK SLPKLVHAKE GFQGCLASVD
LNGRLPDLIS DALFCNGQIE RGCEGPSTTC QEDSCSNQGV CLQQWDGFSC DCSMTSFSGP
LCNDPGTTYI FSKGGGQITY KWPPNDRPST RADRLAIGFS TVQKEAVLVR VDSSSGLGDY
LELHIHQGKI GVKFNVGTDD IAIEESNAII NDGKYHVVRF TRSGGNATLQ VDSWPVIERY
PAGNNDNERL AIARQRIPYR LGRVVDEWLL DKGRQLTIFN SQATIIIGGK EQGQPFQGQL
SGLYYNGLKV LNMAAENDAN IAIVGNVRLV GEVPSSMTTE STATAMQSEM STSIMETTTT
LATSTARRGK PPTKEPISQT TDDILVASAE CPSDDEDIDP CEPSSGGLAN PTRAGGREPY
PGSAEVIRES SSTTGMVVGI VAAAALCILI LLYAMYKYRN RDEGSYHVDE SRNYISNSAQ
SNGAVVKEKQ PSSAKSANKN KKNKDKEYYV
//
