ID A0A1S3EZ84_DIPOR Unreviewed; 1571 AA.
AC A0A1S3EZ84;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Neurexin 3 isoform X2 {ECO:0000313|RefSeq:XP_012869731.1};
GN Name=Nrxn3 {ECO:0000313|RefSeq:XP_012869731.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012869731.1};
RN [1] {ECO:0000313|RefSeq:XP_012869731.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012869731.1};
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_012869731.1; XM_013014277.1.
DR STRING; 10020.ENSDORP00000002718; -.
DR GeneID; 105984164; -.
DR CTD; 9369; -.
DR OMA; TDLKFGS; -.
DR OrthoDB; 2999458at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0097107; P:postsynaptic density assembly; IEA:Ensembl.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
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:UP000081671};
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 1498..1518
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..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1571
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 1553..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1571 AA; 173448 MW; 3ED3F61BF73AD85E CRC64;
MSFTFHSVFF TLKVSILLGS LLGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETAMLS NKQVNDSSWH FLMVSRDRLR
TVLVLDGEGQ SGELHAQRPY MDVVSDLFLG GVPSDIRPSA LTLDGVQAMP GFKGLILDLK
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 PQERKDARSQ KNTKVDFFAV ELLDGNLYLL LDMGSGTIKV KATQKKANDG
EWYHVDIQRD GRSGTISVNS RRTPFTASGE SEILDLEGDM YLGGLPENRA GLILPTELWT
AMLNYGYVGC IRDLFIDGRS KNIRQLAEMQ NAAGVKSSCS RMSAKQCDSY PCKNNAVCKD
GWNRFICDCT GTGYWGRTCE REASILSYDG SMYMKIIMPM VMHTEAEDVS FRFMSQRAYG
LLVATTSRDS ADTLRLELDG GRVKLMVNLD CIRINCNSSK GPETLYAGQK LNDNEWHTVR
VVRRGKSLKL TVDDDVAEGT MVGDHTRLEF HNIETGIMTE KRYISVVPSS FIGHLQSLVF
NGLLYIDLCK NGDIDYCELK ARFGLRNIIA DPVTFKTKSS YLSLATLQAY TSMHLFFQFK
TTSADGFILF NSGDGNDFIA VELVKGYIHY VFDLGNGPNV IKGNSDRPLN DNQWHNVVIT
RDNSNTHSLK VDTKVVTQVI NGAKNLDLKG DLYMAGLAQG MYSNLPKLVA SRDGFQGCLA
SVDLNGRLPD LINDALHRSG QIERGCEGPS TTCQEDSCAN QGVCMQQWEG FTCDCSMTSY
SGNQCNDPGA TYIFGKSGGL ILYTWPANDR PSTRSDRLAV GFSTTVKDGI LVRIDSAPGL
GDFLQLHIEQ GKIGVVFNIG TVDISIKEER TPVNDGKYHV VRFTRNGGNA TLQVDNWPVN
EHYPTGNTDN ERFQMVKQKI PFKYNRPVEE WLQEKGRQLT IFNTQAQIAI GGKDKGRLFQ
GQLSGLYYDG LKVLNMAAEN NPNIKINGSV RLVGEVPSIL GTTQTTSMPP EMSTTVMETT
TTMATTTTRK NRSTASIQPT SDDLVSSAEC SSDDEDFVEC EPSTDKSLST SIFEGGYKAH
APKWESKDFR PNKVSETSRT TTTSLSPELI RFTASSSSGM VPKLPAGKMN NRDLKPQPDI
VLLPLPTAYE LDSTKLKSPL ITSPMFRNVP TANPTEPGIR RVPGASEVIR ESSSTTGMVV
GIVAAAALCI LILLYAMYKY RNRDEGSYQV DETRNYISNS AQSNGTLMKE KQASSKSGHK
KQKNKDKEYY V
//
