ID A0A3B5A183_9TELE Unreviewed; 1220 AA.
AC A0A3B5A183;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Contactin-associated protein-like 4 {ECO:0000313|Ensembl:ENSSPAP00000011999.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000011999.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000011999.1}
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 AlphaFoldDB; A0A3B5A183; -.
DR Ensembl; ENSSPAT00000012205.1; ENSSPAP00000011999.1; ENSSPAG00000007603.1.
DR GeneTree; ENSGT00940000160228; -.
DR Proteomes; UP000261400; 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; 2.
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; 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; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1152..1177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..158
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 280..449
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 451..488
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 487..539
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 698..863
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 864..902
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 920..1116
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1188..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 836..863
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1220 AA; 135211 MW; 17F0BA7BE76F6503 CRC64;
MCVCALSGTP VSSLLLLNPS IWYGNLINHF CMLFFVPLSL SLSLSAGAGG WSPLVSDRYQ
WLEVDLGERT KITAVATQGR YGSSDWLTSY LLMFSDTGHN WKQYRQEDSI GSFPGNSNAD
SVVQNKLQQP TFARFLRLIP LDWNPNGRIG LRLEASIQPL KTHLCASQTS SLESRRLASL
GSLLDDQHWH HVAVEQRNAH LNLTVDKHTE KVQIPAEFNH WNIEQTQISF LLKPAISKRN
FHGCLENLLH NGVNLIELVK NNDHQVAGNV TFSCAEPVSV AVTFTGPQSF LQLPGATASS
PGGVSLGFQF RTWNKAGLLL TFDLPQQGGV VWLYLSEARL RLQIHKDGSA LNDGQWHSVD
VASRRSRLIV SVDKEEGGVA HANPSFPVIV GGQLFFGGKN HGLSLDCENP FNVFQGCMRL
LTVDNQPVDL IRVQHRLLGN YSQLQIDMCG IIDRCSPSRC EHGGRCSQSW NVFHCNCSDS
GYSGAICHSA VYEQSCEAYK HNGNTSGHFY IDVDGSGPIR PQLVYCNMTE ENTWMVMQHN
NTELTSVRPS PGVNQHLVHF DYSAQEEQLL AAISQSEHCE QELSYHCRKS RLLNTLEGSP
FSWWLGGPGS GGVQTYWGGA HPGSQQCACG LQGDCVDPQH YCNCDADRME WTEDSGLLTH
KESLPVRSLV LGDIQRPGSE AAYRVGPLRC HGDKNFWNAA FFDKETSYLH FPTFHGELSA
DISFLFKTTA SSGVFLENLG IKDFIRIELS SSTQVLFSFD VGNGPLEVLV ESSDLLNDNR
WHRVRAERNV KEASLRLDDL PVATQEAPAD GHFHLQLNSQ LFIGGTASRQ KGFRGCIRSL
QLNGVTLDLE ERAKITPGVQ PGCPGHCSSY GSLCQNQGRC VERTNGFHCD CGLSAYTGVF
CQTEVSASFK LGTSVSYTFK EPYELSRNSS ALPSSIYSDM TLRGENVSLS FRTNQSPALL
LYVSSYYREY LALLINKHGE QDETLLPSLN PLNNKQFLHV LGSFLKSNVR SLANGQLHTV
SIRRLTDSVS CHFLDWTRKK KNICKKWITS SPVKLYLIFF SESDDLDPDL ARLASLGFAG
CLSVVQFNTI SPLKAALLHP DTSPVIISGP LVQSNCGSAA SANPHAEENT HHLSGRRWRR
QPLVNAIRTD SALIGGVIAV AIFVTVTALA VAARFLYRRK ETYRNQEVKG VKQEDSQDFS
FNNQVDSQNV STENPKEFFI
//
