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Database: UniProt
Entry: I3N2P6_ICTTR
LinkDB: I3N2P6_ICTTR
Original site: I3N2P6_ICTTR 
ID   I3N2P6_ICTTR            Unreviewed;      1313 AA.
AC   I3N2P6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Contactin-associated protein-like 3 {ECO:0000313|Ensembl:ENSSTOP00000018642.2};
GN   Name=LOC101975743 {ECO:0000313|Ensembl:ENSSTOP00000018642.2};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000018642.2, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000018642.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AGTP01104965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01104966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01104967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01104968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01104969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01104970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 43179.ENSSTOP00000018642; -.
DR   Ensembl; ENSSTOT00000021277.2; ENSSTOP00000018642.2; ENSSTOG00000006516.3.
DR   eggNOG; KOG3516; Eukaryota.
DR   GeneTree; ENSGT00940000157674; -.
DR   HOGENOM; CLU_003504_1_0_1; -.
DR   InParanoid; I3N2P6; -.
DR   OrthoDB; 4255614at2759; -.
DR   TreeFam; TF321823; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:SF36; CONTACTIN-ASSOCIATED PROTEIN-LIKE 3-RELATED; 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; 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   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1313
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011977291"
FT   TRANSMEM        1246..1269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..177
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          183..364
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          370..546
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          548..585
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          584..635
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   DOMAIN          792..957
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          958..996
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1018..1204
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          1219..1238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        930..957
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   1313 AA;  143572 MW;  97B4FC8086CE7F50 CRC64;
     MDPVAGALLK MLALLSAQTC SKVVAGNTYN CNAPLASALP RVSFSSSSEL SSSHGPGFAS
     LNRRDGAGGW TPLVSNKYQW LQIDLGERMK VTAVATQGGY GSSDWVTRYL LMFSDSGRNW
     KQYRREESFW GFPGNTNSDS VVHYRLQPPL EARFLRFLPL AWNSKGRIGM RIEVYGCAYR
     SEMVNFDGKS FLLYTINQKS ISSMKEIITL KFKTRQSDGI LLHREGQNGK HITLELVKGK
     LILFFNSGGA NLPSLDAQVT LTLGSLLDDQ HWHSVLIEVL NTHINFTVDK HTHRFQAEGE
     ASLLDLGYKI SFGGIPGLGK SLVFPHKSFN GCFENLFYNG VDIIDLSKKH KPEILIMGNM
     SFSCSHPQTV PVTFLSSRSY LALPHPTGEN SVAVTFQFRT WNRAGLLLKS QFLHWSGALV
     LVLSDGKLKL SLCPPGQPVR AVIAGDGLND GQWHSVSLSA NGNHLSLKVD NDASSAAHSR
     RGQIHSANTY YFGGYPDNSS GSQCENPLRG FQGCLKLISI GGTVVDPISV QQGELGNFRD
     LQIDSCGITD RCLPSYCEHG GECSQSWDTF SCDCTHTGYV GATCHSSLYE RSCEAYKHRG
     NSSGFYYIDS DGSGPLGPAL VYCNMTDSAW TSVQHNGSHL ARVKSSHGES PQPVIFKYMA
     SMDQLQALID QADHCQQELA FHCKKSRLSA HLDGTPVSWW VGRTNETHTY WGGSLPDAQK
     CTCGLEGNCI DSQYHCNCDA DQDEWTSDTG VLSHKEHLPV TQVMMTDAGR PQSEAAYTLG
     PLLCRGDNSF WNSASFNTET SYLHFPTFRG ELSADVSFFF KTTASSGVFV ENLGITDFIR
     LELRAPTEVT FSFDVGNGPC EVTVQSPTPF NDNRWHHVKA ERNVKEASLQ VDQLPQKFQP
     APTGGHLLLQ LNSQLFIGGT ASRQRGFLGC IRFLQLNGIA LDLEGRAKVT PGVEAGCAGH
     CSSYGHLCHN GGRCQERHRG VACDCTSSAY EGPFCSHEIS AYFGAGSSII YSFQEHHNYT
     FNGNSSSLAA LFHEELTLTR EIVTLSFRTT GTPSLLLFVS SVYEEYLSVI LASNGSLQIR
     YKLDRHREPD VFNFDFKNLA DGQLHNVKIN REAAVVFVEV NQNARRRATL SSGMEFNAVK
     SLVLGMILEP PGADPDTQRA AARGFTGCLS AVRFSHAAPL KAALRLGGPV PVTVHGQVAA
     GSRCAAGAGP GSRVRELAPR LSDGSGYSGP TDEGEPLINA DRSDSAVIGG VVAVVIFILL
     CVTAIAIRIC QQRWLYQKNE SDISKAGDNA EIALKSELNM QNTVSESQKE YFF
//
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