ID A0A3Q3M9D1_9LABR Unreviewed; 1208 AA.
AC A0A3Q3M9D1;
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 5 {ECO:0000313|Ensembl:ENSLBEP00000017050.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000017050.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000017050.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the correct development and proper
CC functioning of the peripheral and central nervous system and be
CC involved in cell adhesion and intercellular communication.
CC {ECO:0000256|ARBA:ARBA00003165}.
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; A0A3Q3M9D1; -.
DR STRING; 56723.ENSLBEP00000017050; -.
DR Ensembl; ENSLBET00000018015.1; ENSLBEP00000017050.1; ENSLBEG00000012989.1.
DR GeneTree; ENSGT00940000160532; -.
DR InParanoid; A0A3Q3M9D1; -.
DR Proteomes; UP000261660; 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; 2.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 3.
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:SF46; CONTACTIN-ASSOCIATED PROTEIN-LIKE 5; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
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 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:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1145..1166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..137
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 143..323
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 330..500
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 502..539
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 538..590
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 747..912
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 913..951
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 968..1126
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 885..912
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1208 AA; 134684 MW; E8ED5EAD2FEBECAC CRC64;
QSSFQSSSQS TASSAAHNAK INRRDGAGGW SPLVTDREPW LQVDLKEQME VTAVATQGRS
ASSDWVSRYL LLYSDTGQVW REYRQEDGGG MFVGNVNSEA VVQNKLSPSL RTHFLRFVPL
DWNPSGWLGL RVELYGCSYK SDVADFDGRS SLLYRFNQKS MSTVKDVISL RFKSRQAEGV
LLHGEGQRGD YITLELHRGK LALYLNLDDT RLRFSSSRVA VTLGSLLDDQ HWHSVTIERF
NKQVNLSVDT HTQHFTTRGE GYSLEVDYEL SFGGIPLPGK PGTFLRRNFD GCIENLYYNG
INIIDLAKRR KPQIYSGNVT FTCSRPSLVA VTFLSSSGSF LSLPMASPLT TLGGFSVRFQ
FRTWNADGLL VSARLSRENQ RLDLQIRNNR LILTIHDQGE RAETSAVNDG LWHSVSLDTR
GLQVSLTLDN EPASTLERWE QLEVRGSFYF GGTPPAARHR PTVSFQGCMR FISINSQTIN
LHHVQQGMLG VYSDLQFDTC SIRDRCVPNL CEHGGVCLQS WSSFSCDCSG TGYSGAVCHH
PLYESSCEAY RLTGGSSGFY SIDPDGSGPL GPAPVYCNMT EERVWTVVRH NVSAPVRVQG
SSLQNPHIMT LNYSSDPKQL HTIIRSSEHC QQEVVYSCRK SRLFNTKDGR PMSWWVDPGG
ERRSYWGGFL PGVQQCSCSL EQNCVDMNYF CNCDADSQSW TNDSGILSYK NHLPVSHIVI
GDTNRTGSEA VYSIGPLRCY GNRWIWNAVS FFQESSSLLF PQLQAELSSD FSFFFKTSAP
SGVFLENLGH KDFIRLELSS PSVVTFSLDV GDGPVVVAVT SPLPLNDRQW HQVRAERNVK
EVWLQVDQLP LRLLEAPADG HRRLRLNGQL VVGGSASRLR GFLGCMRTLN INGVMFDLEE
KARTVVGASS GCPGYCSGSS SLCHNRGRCI EMSNGYTCDC STSAFRGPTC REGESKLHRE
SSLTFTFQEP FSVMQNRSFQ TSGVSRESSS SGTREDVALS FITSHSPAHL LTISTFSQQY
IAVILTTNGT HPRYSRNPDV FSPVLSSLAD GQLHRIRIQR EGRDLYVQVR YRRESFHEEV
VRAGSEGFVG CLSSVQFNHV APLKAALQNR GSSLVTIRGS LVQSNCGTLA NSITSHNLRG
NTQGVVTAAV FITVCILAVV TRLLYLRQVQ KNNDSMQEKE HHHSMETPIR TELHLHNAVR
DNVKEYYI
//
