ID Q8WX98_HUMAN Unreviewed; 1311 AA.
AC Q8WX98;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE SubName: Full=Cell recognition protein CASPR4 {ECO:0000313|EMBL:AAL68839.1};
GN Name=CASPR4 {ECO:0000313|EMBL:AAL68839.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAL68839.1};
RN [1] {ECO:0000313|EMBL:AAL68839.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AAL68839.1};
RX PubMed=12093160; DOI=10.1006/mcne.2002.1110;
RA Spiegel I., Salomon D., Erne B., Schaeren-Wiemers N., Peles E.;
RT "Caspr3 and Caspr4, two novel members of the Caspr family are expressed in
RT the nervous system and interact with PDZ domains.";
RL Mol. Cell. Neurosci. 20:283-297(2002).
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 EMBL; AF463518; AAL68839.1; -; mRNA.
DR PeptideAtlas; Q8WX98; -.
DR ChiTaRS; CNTNAP4; human.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR15036:SF40; CONTACTIN-ASSOCIATED PROTEIN-LIKE 4; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 2: Evidence at transcript level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1311
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004315784"
FT TRANSMEM 1244..1268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..180
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 186..367
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 373..550
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 552..589
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 588..639
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 796..961
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 962..1000
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1012..1205
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 934..961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1311 AA; 145660 MW; 3188BDFE4248208A CRC64;
MLLFYLLVVL SIDSTKASAL TNPNVALFLL ADDCDDPLVS ALPQASFSSS SELSSSHGPG
FARLNRRDGA GGWSPLVSNK YQWLQIDLGE RMEVTAVATQ GGYGSSNWVT SYLLMFSDSG
WNWKQYRQED SIWGFSGNAN ADSVVYYRLQ PSIKARFLRF IPLEWNPKGR IGMRIEVFGC
AYRSEVVDLD GKSSLLYRFD QKSLSPIKDI ISLKFKTMQS DGILLHREGP NGDHITLQLR
RARLFLLINS GEAKLPSTST LVNLTLGSLL DDQHWHSVLI QRLGKQVNFT VDEHRHHFHA
RGEFNLMNLD YEISFGGIPA PGKSVSFPHR NFHGCLENLY YNGVDIIDLA KQQKPQIIAM
GNVSFSCSQP QSMPVTFLSS RSYLALPDFS GEEEVSATFQ FRTWNKAGLL LFSELQLISG
GILLFLSDGK LKSNLYQPGK LPSDITAGVE LNDGQWHSVS LSAKKNHLSV AVDGQMASAA
PLLGPEQIYS GGTYYFGGCP DKSFGSKCKS PLGGFQGCMR LISISGKVVD LISVQQGSLG
NFSDLQIDSC GISDRCLPNY CEHGGECSQS WSTFHCNCTN TGYRGATCHN SIYEQSCEAY
KHRGNTSGFY YIDSDGSGPL EPFLLYCNMT ETAWTIIQHN GSDLTRVRNT NPENPYAGFF
EYVASMEQLQ ATINRAEHCE QEFTYYCKKS RLVNKQDGTP LSWWVGRTNE TQTYWGGSSP
DLQKCTCGLE GNCIDSQYYC NCDADRNEWT NDTGLLAYKE HLPVTKIVIT DTGRLHSEAA
YKLGPLLCRG DRSFWNSASF DTEASYLHFP TFHGELSADV SFFFKTTASS GVFLENLGIA
DFIRIELRSP TVVTFSFDVG NGPFEISVQS PTHFNDNQWH HVRVERNMKE ASLQVDQLTP
KTQPAPADGH VLLQLNSQLF VGGTATRQRG FLGCIRSLQL NGMTLDLEER AQVTPEVQPG
CRGHCSSYGK LCRNGGKCRE RPIGFFCDCT FSAYTGPFCS NEISAYFGSG SSVIYNFQEN
YLLSKNSSSH AASFHGDMKL SREMIKFSFR TTRTPSLLLF VSSFYKEYLS VIIAKNGSLQ
IRYKLNKYQE PDVVNFDFKN MADGQLHHIM INREEGVVFI EIDDNRRRQV HLSSGTEFSA
VKSLVLGRIL EHSDVDQETA LAGAQGFTGC LSAVQLSHVA PLKAALHPSH PDPVTVTGHV
TESSCMAQPG TDATSRERTH SFADHSGTID DREPLANAIK SDSAVIGGLI AVVIFILLCI
TAIAVRIYQQ KRLYKRSEAK RSENVDSAEA VLKSELNIQN AVNENQKEYF F
//
