ID A0A3B3UTV9_9TELE Unreviewed; 1266 AA.
AC A0A3B3UTV9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Contactin-associated protein-like 5 {ECO:0000313|Ensembl:ENSPLAP00000016308.1};
GN Name=CNTNAP5 {ECO:0000313|Ensembl:ENSPLAP00000016308.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000016308.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000016308.1}
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; A0A3B3UTV9; -.
DR STRING; 48699.ENSPLAP00000016308; -.
DR Ensembl; ENSPLAT00000025201.1; ENSPLAP00000016308.1; ENSPLAG00000022248.1.
DR GeneTree; ENSGT00940000160532; -.
DR Proteomes; UP000261500; 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; cd00053; EGF; 1.
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 NCBIfam; NF040941; GGGWT_bact; 1.
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; 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; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1198..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..154
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 160..344
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 351..524
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 526..563
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 562..614
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 771..936
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 937..975
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 997..1178
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 909..936
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1266 AA; 141451 MW; DC2F0C0F0EA009C3 CRC64;
MFCFPDNCNG PLASALPHSS FQSSSQSSAG YSAFYAKLNR RDEAGGWSPM VTDQDPWLQV
DLREQMEVTA VATQGRYDSS DWVSSYLLLY SDTGRIWKQY RHEDGLERFD GNVNSETVVQ
NKLSHPVKTR FLRFVPLDWN PSGWMGLRVE VFGCSYKSYV ADFDGRSSLL YRFNQKSMST
VKDVISLRFK SHQAEGVLLH GEGQRGDYIT LELHRGRLDL YLNLGELHDS RSRFSSRRVP
VTVGSLLDDQ HWHSAQIERF NRQVNLTVDA HTQHFQTKGE GQSLEVDYEL SFGGIPLPGK
PGTFLRKNFH GCIENLYYNG INIIDLAKRR KPQIHSVGNV TFSCSPPQLV ACTFLSSTSS
FLSLPSAAPA TGEFTVRFQF RTWNPDGLLL SVQLNPSPQK LDLEGKLNYV NNLYYPYLLK
LIILCCLGRR VNDGLWHAVS LASRSLQITL SVDGEPSSDV ELWEPVESRG SLYFGGCPPT
ECHIQAPAFQ GCMQLISINN HLVNLSHVQQ GLLGNYNELQ FDTCNMKDRC LPNLCEHGAR
CSQTWSSFSC DCSGTGYSGA TCHNSIHESS CEAYKLSGSS SGFYFIDPDG SGPLGPTQVY
CNMTEKKVWT VLSHNNSAPV KVQNSSPQRP HVMKFSYNAS ADQLRAIVTG AEQCQQEVVY
NCRKSRLFNT KDGSPLSWWL DRQGDKRSYW GGFLPGVQQC SCSLEENCMD MNYFCNCDAD
ADAWTNDTGI LSYKDHLPVS QIVIGDTNRT GSQAVYHVGS LRCYGDKSIW NAASFYQESS
YLYFPTLQAE LASDISFYFK TSSPSGVFLE NQGLKDFIRV ELSSPTVVTF SFDVGNGPAV
LSVKSHLPLN DRQWHYVRAE RNVKEASLQV DQLPLRLLQA PADGHLRLRL SSQLFVGGTA
SQQRGFLGCI RSLMVNGMTF DLEERAKMTP GVSSGCPGYC SGSSNLCHNR GRCIEKSNGY
ICDCSQSAYG GATCNQEVSV SFDRDSSVTY TFQEPFSVMQ NRSSQASSAF AESRAREDMA
FSFVTSQRPA MLLTISTFTQ QYITTILARN GKNGYNLQIW YHLQTDRSPD VFNPTPKNLA
DGRLHRIRIH RVGKNLYIDQ DIHRKYTLSS DAELILIRSL TLGKVISKLS NLRRTASKGF
VGCLSSVQFN HVAPLKAALT NRGSSLITIR GPLVQSNCGA LAESTSHDQH DSNAQKDLAV
IAGVVTAVVF IAVCALAVIS RLLYQQRRAK RSSGMKEEHR HSTYTDYRTE LHLHNSVRDN
VKEYYI
//
