ID A0A3Q0DCN6_MESAU Unreviewed; 1676 AA.
AC A0A3Q0DCN6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Neurexin 3 isoform X3 {ECO:0000313|RefSeq:XP_021090862.1};
GN Name=Nrxn3 {ECO:0000313|RefSeq:XP_021090862.1};
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_021090862.1};
RN [1] {ECO:0000313|RefSeq:XP_021090862.1}
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_021090862.1; XM_021235203.1.
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 1603..1623
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 262..444
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 451..643
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 647..684
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 689..861
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 875..1050
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1053..1090
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1094..1294
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1328..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1676 AA; 184420 MW; C7F7B74BDD7CA3ED 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 EQGRSKAREE NVATFRGSEY LCYDLSQNPI QSSSDEITLS FKTWQRNGLI
LHTGKSADYV NLALKDGAVS LVINLGSGAF EAIVEPVNGK FNDNAWHDVK VTRNLRQVTI
SVDGILTTTG YTQEDYTMLG SDDFFYVGGS PSTADLPGSP VSNNFMGCLK EVVYKNNDIR
LELSRLARIG DTKMKIYGEV VFKCENVATL DPINFETPEA YISLPKWNTK RMGSISFDFR
TTEPNGLILF THGKPQERKD VRSQKNTKVD FFAVELLDGN LYLLLDMGSG TIKVKATQKK
ANDGEWYHVD IQRDGRSGTI SVNSRRTPFT ASGESEILDL EGDMYLGGLP ENRAGLILPT
ELWTAMLNYG YVGCIRDLFI DGRSKNIRQL AEMQNAAGVK SSCSRMSAKQ CDSYPCKNNA
VCKDGWNRFI CDCTGTGYWG RTCEREASIL SYDGSMYMKV IMPMVMHTEA EDVSFRFMSQ
RAYGLLVATT SKDSADTLRL ELDGGRVKLM VNLDCIRINC NSSKGPETLY AGQKLNDNEW
HTVRVVRRGK SLKLTVDDDV AEGTMVGDHT RLEFHNIETG IMTEKRYISV VPSSFIGHLQ
SLMFNGLLYI DLCKNGDIDY CELKARFGLR NIIADPVTFK TKSSYLTLAT LQAYTSMHLF
FQFKTTSADG FILFNSGDGN DFIAVELVKG YIHYVFDLGN GPNVIKGNSD RPLNDNQWHN
VVITRDNSNT HSLKVDTKVV TQVINGAKNL DLKGDLYMAG LAQGMYSNLP KLVASRDGFQ
GCLASVDLNG RLPDLINDAL HKSGQMERGC EGPSTTCQED SCANQGVCMQ QWEGFTCDCS
MTSYSGNQCN DPGATYIFGK SGGLILYTWP ANDRPSTRSD RLAVGFSTTV KDGILVRIDS
APGLGDFLQL HIEQGKIGVV FNIGTVDISI KEERTPVNDG KYHVVRFTRN GGNATLQVDN
WPVNEHYPTG NTDNERLQMV KQKIPFKYNR PVEEWLQEKG RQLTIFNTQA QIAIGGKDKG
RLFQGQLSGL YYDGLKVLNM AAENNPNIKI NGSVRLVGEV PSVSGTTQTT SMPPEMSTTV
METTTTMATT TTRKNRSTAS IQPTSDDLVS SAECSSDDED FVECEPSTGG ELVIPLLVED
PLATPPIATR VPSITLPPTF RPLLTIIETT KDSLSMTSEA GLPCLSDQGS EGCDDDGLVI
SGYGSGETFD SNLPPTDDED FYTTFSLVTD KSLSTSIFEG GYKAHAPKWE SKDFRPNTVS
ETSRTTTTSL SPELIRFTAS SSSGMVPKLP AGKMNNRDLK PQPDIVLLPL PTAYELDSTK
LKSPLITSPM FRNVPTANPT EPGIRRVPGA SEVIRESSST TGMVVGIVAA AALCILILLY
AMYKYRNRDE GSYQVDETRN YISNSAQSNG TLMKEKQASS KSGHKKQKNK DKEYYV
//
