ID A0A3P8ZFV7_ESOLU Unreviewed; 1250 AA.
AC A0A3P8ZFV7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Contactin associated protein-like 5a {ECO:0000313|Ensembl:ENSELUP00000027646.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000027646.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000027646.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000027646.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8ZFV7; -.
DR Ensembl; ENSELUT00000015417.2; ENSELUP00000027646.2; ENSELUG00000004224.2.
DR GeneTree; ENSGT00940000160532; -.
DR Proteomes; UP000265140; LG16.
DR Bgee; ENSELUG00000004224; Expressed in brain and 2 other cell types or tissues.
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; 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:SF46; CONTACTIN-ASSOCIATED PROTEIN-LIKE 5; 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; 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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1184..1209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..127
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 133..313
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 320..494
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 496..533
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 532..584
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 741..906
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 907..945
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 965..1152
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 879..906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1250 AA; 138956 MW; FFF404804C8E7FA0 CRC64;
FLSVIAGQLG GSGSPNSGGW SPQATDRQPW MQLDLKDRME VTAIATQGRY GSSDWVSGYL
LLFSDTGRAW KQYREEDGVG RFVGNVNPND VVHHKLSHSI RSRFLRFVPL DWNPSGWVGL
RVEVYGCAYK SDVTDFDGRS SLLYRFNQKS MSTVKDVISL RFKSRQAEGV LLHGEGQRGD
YITLELHRGR LALYLNLDDT RLRFSSGRVA VTLGSLLDDQ HWHSVLIERF NKQVNFTVDS
HTEHFRTKGE GVSLEVDYEL SFGGIPLPGK PGTFLRKNFH GCIENLYYNG INVIDLAKRR
KPQIYSGNVT FSCSEPQLVS TTFLSSSSSF LSLRATASSL GGFAVRFRFR TWNPDGLLLS
TRLALEPQRL ELQISNSRLR LTHHTSAQQK EEVSTGHRVN DGLWHSVSLS SRGLQVTMTL
DNEPPSTIDL EDHMEAGDLY FGGCPSVNVA GCVNPTLAFQ GCMRLISVNS QPIDLNLLRQ
GRLGNYRELQ FNTCGIHDRC LPNFCEHAGQ CSQSWSTFYC DCSGTGYNGA TCHNSIYEVS
CEAYRLAGSS SGYFSIDPDG SGPLGPTKVY CNMTEDKVWT VVTHNSTDPI RVQGSTLQKP
YIMKFNYSAS PEQLIALVAG SEQCQQEVTY SCRKSRLFNT RDGTPLSWWV DQAGERRTYW
GGFLPGVQQC SCSLEENCID MNYFCNCDAD TDSWANDTGV LSYKEHLPVS EIVIGDTNRT
FSEALYRIGP LRCYGDKSTW NAASFYQESS YLHFPTLQTE LSADLSFYFK TSAPSGVFLE
NLGLKDFIRV ELSSPSVVTF SFDVGNGPVI LAVKSHVPLN DRQWHCVRAE RSVKEASLQV
DQLPLRFLEA PSDGHLRLRL NSQLFVGGTA ARQRGFLGCI RTLTINGVTV NLEERAKMTP
GVSPGCPGHC SSSSSLCHNR GRCVEKNSGY VCDCSQSAYG GSSCTEEVSV SFDRESSVTY
TFQEPFSVMQ NRSSQASSWY RESSRARENM AFSFMTTQSP AMLLTVSTFS QQYIAVILAR
NGSLQIWYHL HVDRRPDVFS PRPSSLADGR LHRIRLHREG RYIYLQVSQE MECIAPLSAY
LTSEAELISI KSLALGKVTE AVSEDVMWAG SKGFIGCLSS VQFNRVAPLK AALLNHGSSL
VSIRGQLVES NCGLLADSAI LHSQSETVGR GKEPLRNASQ SNSAVIGGVV TTVVFITLCA
VAVMTRFLYR HRQGRTDASV TEKEHRHNLE TAYRRETAYQ AEPCKATELV
//
