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Database: UniProt
Entry: A0A2D0Q867_ICTPU
LinkDB: A0A2D0Q867_ICTPU
Original site: A0A2D0Q867_ICTPU 
ID   A0A2D0Q867_ICTPU        Unreviewed;      1313 AA.
AC   A0A2D0Q867;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 2.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Contactin-associated protein-like 5 isoform X1 {ECO:0000313|RefSeq:XP_017314492.2};
GN   Name=cntnap5b {ECO:0000313|RefSeq:XP_017314492.2};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017314492.2};
RN   [1] {ECO:0000313|RefSeq:XP_017314492.2}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017314492.2};
RG   RefSeq;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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   RefSeq; XP_017314492.2; XM_017459003.3.
DR   STRING; 7998.ENSIPUP00000009310; -.
DR   Ensembl; ENSIPUT00000009717; ENSIPUP00000009310; ENSIPUG00000006377.
DR   KEGG; ipu:108259481; -.
DR   OMA; CTEPHIV; -.
DR   OrthoDB; 4255614at2759; -.
DR   Proteomes; UP000221080; Chromosome 27.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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; 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   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..1313
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039941414"
FT   TRANSMEM        1258..1283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..190
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          196..377
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          384..567
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          569..606
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          605..657
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   DOMAIN          814..979
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          980..1018
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1036..1223
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          1228..1254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1228..1253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        952..979
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   1313 AA;  145743 MW;  DB8C6621BBD1FA40 CRC64;
     MMMKMTMMRT VSFGVGARRT FLALVLAVLC ALRSARSAHH HHHCNGPLLS LLPPTSFHSS
     SVSSESHAGY YAKLNNRDGG GGWRPDHTDR LRWLQVDLRE RMEIIAVATQ GASGSSDWVT
     RYTLLYSDTG RDWKQYRHED YAGVFPGNTD ADGVVHHKLP HAIRTRYLLF LPQDWSAEGW
     IGLRVEAYGC SYKSDLADFD GRSALLYRFN QKSMSTVKDV ISLQFKSVRS DGVLVHGEGQ
     RGDYITLELQ RGRLALHINL DDAKAHPSSA HVSISLGSLL DDQRWHSVLI ERFNKQINFT
     VDRMTRHLRS GGIGDSLEVD YELSIGGVPL PGKPGTFLRK NFHGCMENLY YNGVNIIDLA
     KRKKPQIYSV GNVTFSCSEP PAVSATFLSS SSSFLQAPAD LSAMTETDSG ETSGWSAGFQ
     FRTWNRDAML MWIGLQGVEK LVLLLSDAQL RLTHHRSALQ SSEITVGRSL SDGLWHSVSL
     TLKENQASVS VDNDSPSSMM LGRHARPGNT VLIGGCPASA TNQGCRNPTL AYQGCMRSIV
     LNNRPLDLYR VQQGLLGNYS GLQIDICGIQ DRCLLNYCEH GGECSQSWSS FSCDCSGTGY
     TGATCHNSIF EMSCEAHRLA GSSSGFFSID PDGSGPLTHT VVYCNMSEEK VWMVIGHNNS
     KPVSVQGSSF QKPHVMKLNY SASLQQLTTL LHRAQHCQQE VVYRCRKSRL FNTWDGTPLS
     WWKDRAGEKR TYWAGLLPGV QQCSCSLAEN CIDMNHFCNC DADRSSWEND TGLLSYKEHL
     PVTEMVVGDT NRSGSEAVYR VGSLQCHGDR FLWNAVSFYQ ESSSLHYATL HAELSVDISF
     YFKTTAPSGV FLENLGVRDF IRLELSAPST VAFSFDVGSG PLVLTVKSHV PLNDKQWHHV
     RAERNVKEAS LQVDQLPLRF LEAPHDGHAR LQLNGQLFIG GTASRQKGFL GCIRALTING
     MSLDLEERAK MTPGVSAGCP GHCSSQNRLC HNRGRCIERN SGYVCDCTHS AYGGPRCQTE
     VSVSFESGTS VTYTFQEPFS VTRNTSVQSS AIYAQSSRSR ENIAFRFLTT KSPAMLMTVT
     TYQQQYMAII LARNGSLQIW YKLKREMEPD VFTATEYNLA NGQLHRVQLH REGGDMYVQV
     DKDASQKYGL STDQELNLIR SLTLGKVTSR AGVDEEVLQA GAKGFIGCLS SVQFNHLAPL
     KAAILNRGSS LVSVLGNLVE SNCGELADRS HSHSLSDHTD GEKRGKERLK NSEPSDSAVI
     GGLIAALLLV VLCIMAVMMR FLLRFRRERS RQPKEKDLRA QSELRDSRKE YFI
//
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