ID A0A1S3RH53_SALSA Unreviewed; 1718 AA.
AC A0A1S3RH53;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Neurexin 3 isoform X4 {ECO:0000313|RefSeq:XP_014051620.1};
GN Name=nrxn3 {ECO:0000313|RefSeq:XP_014051620.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014051620.1};
RN [1] {ECO:0000313|RefSeq:XP_014051620.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014051620.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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_014051620.1; XM_014196145.1.
DR OrthoDB; 2999458at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
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; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR PANTHER; PTHR15036:SF57; NEUREXIN-3; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 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; 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|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1718
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010291853"
FT TRANSMEM 1644..1664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..201
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 197..234
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 280..462
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 469..662
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 666..703
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 708..880
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 894..1069
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1081..1118
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1122..1322
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1353..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1718 AA; 189042 MW; 7D8B3CA171B47DDD CRC64;
MDVLGLSARL QLLLSALLGV CLSLEFTGAP GQWARYLRWD ASTRSDLSFQ FKTDVSTALL
LYFDDSGYCD FLQLMVVEGK LQLRFSIDCA ETAVVSDKRV NDSSWHFATL SRYGLRTVLG
LDGQVKADEV RPTGGSRQHM KIVSDLFLGG VPLDIRMSAL TLPTARDAPP FRGTISDLKY
GNTEPVLLSS LRVRLESEGR CTENPCENSG SCTVVDGEPM CDCSKTEYKG RFCNEEVNNN
IPGFSHMMMA EQAKSKGTDQ SFSYPRFKKP WARLTREENV ATFRGSEYFC YDLSQNPIQS
SSDEITLSFK TWQRNGLILH TGKSADYVNL ALKDGAVSLV INLGSGAFEA IVEPVNGKFN
DNTWHDVKVT RNLRQVTISV DGILTTTGYT QEDYTMLGSD DFFYVGGSPS TADLPGSPVS
NNFMGCLKEV VYKNNDIRLE LSRLARIVDP KMKIQGDVVF KCENVATLDP ISFETPEAYI
SLPKWNTKRM GSISFDFRTS EPNGLILFTH GKPQERKEAQ RSQKNTKVDF FAVELLDGSL
YLLLDMGSGT IKVKATQNKV NDGAWYHVDI QRDGRSGTIS VNSRRTPFTA SGESEILDLE
GDMYLGGLPS DRANLILPTE LWTAMLNYGY VGCVRDLFID GRSKDIRQIA EAQNGAGIKP
SCNKVVGKQC ESYPCKNKGV CKEGWNRFIC DCTGTGYWSR TCEREASILS YDGSMYMKVV
MPQVMHTEAE DVSLRFMSQR AYGLLMATTS RDSADTLRLE LDGGRVKLTV NLDCIRINCT
SSKGPETLYA GQKLNDNEWH TVRVVRRGKT YKLTVDDDVA EGQMAGDHTR LEFHNIETGI
MTERRFVSAI PSSFIGHLQS LRFNGMLYID LCKNGDIDFC ELNARFGMRS IIADPVTFKS
KSSYLSLATL QAYTSMHLFF QFKTTSPDGF IMFNTGDGND FIAVELVKGY IHYVFDLGNG
PNVIKGNSDR ALHDNQWHNV VITRDNSNIH TLKVDAKATS QVVNGAKNLD LKGDLFIAGL
GAGMYNNLPK LVASRDGFQG CLASVDLNGR LPDLLQDALF RSGQIERGCE VGFTKADLQG
PSTTCQEDSC ANMGVCIQQW ENYTCDCSMT SYTGTQCNDP GMTYIFGKGG GLITFNWPAN
ERPSTRTDRL TIGFSTSLKD GILVRIDSAP GLGDYLMLHI EQGKIGVTFN IGTMDISVRE
SSTPVNDGKY HVVRFTRNGG NATLQVDNWS INEHFPGATT DNERLEIATK KFPLKYARPV
VDWLQEKGRQ LTIFNTQATV TIGGSDRSRP FQGQLSGLYY NGLKVLNMAA EGNPNIKING
SVRLVGDVPS VAGSARTTAQ PPEMSTTFIE TTTTMSTTTT RKHRSSPTIQ QTTDDIVSSA
ECSSDDEDLE ECDSGHAGGL GGELVIPVLL EEPLVLPPVA TRAPSIPLPP TLRPPLTIIE
PTKESLSTAT EAGVPCLSDR GSDDCDDDDD GLVISGYGSG EAFNSNLPPT DDEDFYTTFS
LVTDKTLSTS AFEGGYKVHA PKWETKDFSS NKPSSDRGRT TTTAALPLAP DQSRYTSTAT
LHHTPPAKLP AGKMNNRELK PQPDIVLLPL PTLPYEVDST KQRAPVITSP MFRNVPTALP
TQPGVNRVPG PPEVSRQSSS TTGMVVGIVA AAALCILILL YAMYKYRNRD EGSYQVDESR
NYITNSATQS NGAVMKDKQQ SAKGSKVKQK NKDKEYYV
//