ID A0A1U8CHQ8_MESAU Unreviewed; 1467 AA.
AC A0A1U8CHQ8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Neurexin 3 isoform X21 {ECO:0000313|RefSeq:XP_012978991.1};
GN Name=Nrxn3 {ECO:0000313|RefSeq:XP_012978991.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012978991.1};
RN [1] {ECO:0000313|RefSeq:XP_012978991.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion. May mediate intracellular signaling.
CC {ECO:0000256|ARBA:ARBA00043901}.
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_012978991.1; XM_013123537.2.
DR GeneID; 101835363; -.
DR CTD; 9369; -.
DR OrthoDB; 2999458at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
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; 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: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; 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:ARBA00023180};
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:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1394..1414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..202
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 198..235
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 258..440
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 447..639
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 643..680
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 685..857
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 871..1046
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1049..1086
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1090..1290
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1324..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1467 AA; 161941 MW; 237902C2C94969CD CRC64;
MSFTLHSVFF TLKVSIFLGS LVGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETTVLS NKQVNDSSWH FLMVSRDRLR
TGLVIDGEGQ SGMLQPQRPY MDVVSDLFLG GVPADIRPSA LTLDGVQNMP GFKGLMLDLK
YGNSEPRLLG SQGVQLEAEG PCGERPCENG GICFLLDGHP TCDCSTTGYG GTLCSEDVSQ
GPGLSHLMMS EQAREENVAT FRGSEYLCYD LSQNPIQSSS DEITLSFKTW QRNGLILHTG
KSADYVNLAL KDGAVSLVIN LGSGAFEAIV EPVNGKFNDN AWHDVKVTRN LRQVTISVDG
ILTTTGYTQE DYTMLGSDDF FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDIRLELS
RLARIGDTKM KIYGEVVFKC ENVATLDPIN FETPEAYISL PKWNTKRMGS ISFDFRTTEP
NGLILFTHGK PQERKDVRSQ KNTKVDFFAV ELLDGNLYLL LDMGSGTIKV KATQKKANDG
EWYHVDIQRD GRSGTISVNS RRTPFTASGE SEILDLEGDM YLGGLPENRA GLILPTELWT
AMLNYGYVGC IRDLFIDGRS KNIRQLAEMQ NAAGVKSSCS RMSAKQCDSY PCKNNAVCKD
GWNRFICDCT GTGYWGRTCE REASILSYDG SMYMKVIMPM VMHTEAEDVS FRFMSQRAYG
LLVATTSKDS ADTLRLELDG GRVKLMVNLD CIRINCNSSK GPETLYAGQK LNDNEWHTVR
VVRRGKSLKL TVDDDVAEGT MVGDHTRLEF HNIETGIMTE KRYISVVPSS FIGHLQSLMF
NGLLYIDLCK NGDIDYCELK ARFGLRNIIA DPVTFKTKSS YLTLATLQAY TSMHLFFQFK
TTSADGFILF NSGDGNDFIA VELVKGYIHY VFDLGNGPNV IKGNSDRPLN DNQWHNVVIT
RDNSNTHSLK VDTKVVTQVI NGAKNLDLKG DLYMAGLAQG MYSNLPKLVA SRDGFQGCLA
SVDLNGRLPD LINDALHKSG QMERGCEGPS TTCQEDSCAN QGVCMQQWEG FTCDCSMTSY
SGNQCNDPGA TYIFGKSGGL ILYTWPANDR PSTRSDRLAV GFSTTVKDGI LVRIDSAPGL
GDFLQLHIEQ GKIGVVFNIG TVDISIKEER TPVNDGKYHV VRFTRNGGNA TLQVDNWPVN
EHYPTGNTDN ERLQMVKQKI PFKYNRPVEE WLQEKGRQLT IFNTQAQIAI GGKDKGRLFQ
GQLSGLYYDG LKVLNMAAEN NPNIKINGSV RLVGEVPSVS GTTQTTSMPP EMSTTVMETT
TTMATTTTRK NRSTASIQPT SDDLVSSAEC SSDDEDFVEC EPSTGRSANP TEPGIRRVPG
ASEVIRESSS TTGMVVGIVA AAALCILILL YAMYKYRNRD EGSYQVDETR NYISNSAQSN
GTLMKEKQAS SKSGHKKQKN KDKEYYV
//
