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Database: UniProt
Entry: A0A3Q0QWR3_AMPCI
LinkDB: A0A3Q0QWR3_AMPCI
Original site: A0A3Q0QWR3_AMPCI 
ID   A0A3Q0QWR3_AMPCI        Unreviewed;      1285 AA.
AC   A0A3Q0QWR3;
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 3 {ECO:0000313|Ensembl:ENSACIP00000001756.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000001756.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000001756.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   STRING; 61819.ENSACIP00000001756; -.
DR   Ensembl; ENSACIT00000001830.1; ENSACIP00000001756.1; ENSACIG00000000527.1.
DR   GeneTree; ENSGT00940000160228; -.
DR   OMA; WNPAGRI; -.
DR   Proteomes; UP000261340; 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; 4.
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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          94..201
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          207..380
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          386..564
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          566..603
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          602..647
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   DOMAIN          803..968
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          969..1007
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1025..1199
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DISULFID        941..968
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   1285 AA;  141390 MW;  EF39AC6B9D6E2894 CRC64;
     MRAGCERVCV LYGFLTRSAR VLACELSGAL VSSLLLQNSS IWCLSSVSLF WSSNAIHSFL
     LTRTYFISSN LDGNLITYIC IFFYSHLSAG AGGWSPLISD KYQWLEVDLG ERTKITAVAT
     QGRYGSSDWL TSYLLMFSDT GHNWKQYRQE DSIGSFPGNS NADSVVQYKL QQAAIARFLR
     LIPLDWNPSG RIGLRLETYG CPYTSDVVSL NGGSSSLVYR LSPGPWRTSK EVVSLKFKTL
     RNSGMLLHAE GQQGVSLSLE LERGKLQLLL RKGTTQHKHT VMVRLTSLGS LLDDQHWHHV
     VLEQRNAHLN LTVDKNTERV QLPAEFSRWD IEQVSQKPDI SKKNLRGCIE NLLYNNVNLI
     ELAQKRDRQV TVRGNVTFSC AEPVSIALTF PGPQSFLQLP GTTTSSLDGV SVGFQFRTWN
     RAGLLLTFGL LQKGGMVWLY LSDARLRLQI HKGLSPAFSP GAALNDGQWH SVDLTCRRGR
     LTISVDKEEG GIAHATPSFP VTTGSQLFFG GKSDSWLIGE ECRNPFETFQ GCMRLLTVEN
     QPVDPIMVQQ RLLGNYSQLL IDMCGITDRC SPSRCEHGGR CSQSWTVFHC NCSDTGYSGA
     TCHSSVYEQS CEAYKHNGNT SGHFYIDVDG SGPIKPQLVY CNMTGDTHMH THTHLTRVQP
     SPGVSQHSVH FDYSSQEEQL LAAISQSEHC EQELSYHCRK SQGSPFSWWL GGPGQGRVQT
     YWGGAHPGSQ QCACGLQGDC VDLQHYCNCD ADRLEWTEDS GLLTHKDTLP IRSLVLGDIQ
     RPGSEAAYRV GPLRCHGDKN FWNAAFFDKE TSYLHFPTFH GELSADISFL FKTTGSSGVF
     LENLGIKDFI RIELSSSTQV VFSFDVGNGP LEVRVESSVP LNDNRWHRVR AERNVKEASL
     RLDELPVATQ EAPADGHFHL QLNSQLFIGG TASRQKGFRG CIRSLQLNGV TLDLEERAKI
     TPGVQPGCPG HCSSYGSLCQ NQGRCVERAN GFQCDCSLSA HVGVFCQTEV SASFKSGTSV
     IYTFKEPYEL SRNSSALPSS IYSDLTLRGE NVSLSFRTNQ SPALLLYVSS YYREYLALLI
     NRHDKLEVRY KLDSSRDAEV LKSSVKSVAN GQLHTVAIRR LTDSVSVQVK PPHQLITLLL
     DASKESDDLD PDLARLASLG FTGCLSVVHF NAISPLKAAL LHPDTSPVII TGPLVQSNCG
     SAASANPYAA ENTHHLSGKK GGSGSTGSGQ PLINAIRTDS ALIGGTLSII HYAGTFSPCF
     AVELLLNCVG LNISAIRGFL QSLIC
//
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