ID A0A3Q2FR24_CYPVA Unreviewed; 1201 AA.
AC A0A3Q2FR24;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Contactin-associated protein-like 4 {ECO:0000313|Ensembl:ENSCVAP00000008405.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000008405.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000008405.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q2FR24; -.
DR Ensembl; ENSCVAT00000001677.1; ENSCVAP00000008405.1; ENSCVAG00000010477.1.
DR GeneTree; ENSGT00940000160228; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 1.
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; 2.
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 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; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1133..1154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..145
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 287..464
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 466..503
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 502..554
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 713..878
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 879..917
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 921..1105
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1167..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 851..878
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1201 AA; 132277 MW; C750409FE8B23973 CRC64;
SRVLHTWVAW NRGADYYQSQ TFLLSISDQS FNSQSGGWSP LTSDGYQWLE VDLGQRTKIS
AIATQGRYGS SDWLTSYQLM FSDTGHNWKQ YRQEDSIGSF PGNNNADSVV QYKLQQPVVA
RFLRLIPLDW NPSGRIGLRL ETYGCPYTSD VLNLDGSSSL VYRLSPGSRP TQTHVITLKF
KTLRNSGTLL QVDGREGLTL SLEIERGKLL LLFRQGKASS AKLQQLASLA SLLDDQQWHY
VAVELRGQNL NLTVDKHTLG VKIPLKFHHL DIEEGNVTFS CAEPVSAAVT FPGPQSFLQL
PWTASSSSGS ASIGFQFRTW NNAGLLLTFD LPGQGGVVWL FLNEARLYMQ IQKEGRVLLE
LSAGSALSDG QWHSVELNSK QSRLTVSVDK DEGGSAQASL SFPLTVESHL FFGCPSGDIH
GCRNPVTAFQ GCMRLFSLDN RIMDLIAVQQ KHLGNYSNLQ IDMCGIIDRC SPSRCEHGGL
CSQTWSVFHC NCSNSGYGGA TCHSSVYQQS CEAYKHNGNT SGYFYIDVDG SGPIKPQLVY
CNMTDSETWM IIQHNNTELT TVSPAAGLDH HSVHFSYSSE EEQLLGSIIQ SEHCEQELSY
QCRKSRLLNT PEGTPFSWWL GGRAPGRVQT YWGGAHPGSQ QCACGLHGDC VDPQHYCNCD
ADIMEWTEDS GLITHKEHLP IRSLVAGDIQ RPGSEAAYRV GPLRCFGDKN FWNTAFFEKE
TSYLHFPTFH GELSADISFL FKTTASSGVF LENLGIKDFI RIELSSSTRV VFSFDVGNGP
LEVQVESTVP LNDNRWHQVH AERNIKEASL RLDSLPVATQ EAPAEGHVHL QLNSQLFIGG
TASRQRGFRG CIRSLQLNGV TLDLEERAEI TPGVRPGCPG HCSSYGSLCQ NQGRCVERAK
GFNCDCSLSA YTGVFCHTEL SASFKSGTSI RYTFKEPNKM SRNGSALPSS IHSDTTLRGE
NISLSFRTAQ SPALLLYVSS YYSEYMAVLI NKHDKLEVRY KLEGNRDAEV LRSSSGRNLA
DGQLHSITIS RRTHTVSVQV CVLAGTAKTN HSDALDPHLS RLASLGFTGC LSVVQFNSVS
PLKAALLHPD TSPVHITGPL VQSNCGSAAS ANPYSGSVGS GQPLVNAIRT DSALIGGVIA
VVIFVILTGL AIAARHLYQR KDTYRTQEEN RVKQEDCPDF PLNNPNDSQN LSMENPKEYF
I
//
