UniProt: G3SVT1

Database: UniProt
Entry: G3SVT1_LOXAF

LinkDB:  G3SVT1_LOXAF 
Original site:  G3SVT1_LOXAF

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Ontology (1)   
   GO (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (17)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (5)   
   SMART (3)   
All databases (21)   

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ID   G3SVT1_LOXAF            Unreviewed;      1307 AA.
AC   G3SVT1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Contactin associated protein like 5 {ECO:0000313|Ensembl:ENSLAFP00000004373.3};
GN   Name=CNTNAP5 {ECO:0000313|Ensembl:ENSLAFP00000004373.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000004373.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000004373.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004373.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000004373.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004373.3};
RG   Ensembl;
RL   Submitted (NOV-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   STRING; 9785.ENSLAFP00000004373; -.
DR   Ensembl; ENSLAFT00000005225.3; ENSLAFP00000004373.3; ENSLAFG00000005223.3.
DR   eggNOG; KOG3516; Eukaryota.
DR   GeneTree; ENSGT00940000160532; -.
DR   HOGENOM; CLU_003504_1_0_1; -.
DR   InParanoid; G3SVT1; -.
DR   OMA; CIVAIMS; -.
DR   TreeFam; TF321823; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 1.
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:UP000007646};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1307
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003454263"
FT   TRANSMEM        1239..1264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..174
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          180..361
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          368..545
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          547..584
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          583..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          1021..1200
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DISULFID        930..957
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   1307 AA;  145706 MW;  1C28440FC00836BC CRC64;
     MDSIPLLTCV LTLLFSSLWR LGLTATNYKC DDPLASLLSP MAFSSSSDLS GTHSPAQLNR
     RVGTGGWSPA DSNGQQWLQM DLGNRVEITA VATQGRYGSS DWVTSYSLMF SDTGRNWKQY
     KQEDSIWTFA GNMNADSVVH HKLLHSVRAR FIRFVPLRWN PSGKIGMRVE VYGCSYKSDV
     ADFDGRSSLL YRFNQKLMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQKGRLAL
     YLNLDDSKAR ISSNPPSATL GSLLDDQHWH SVLIERVGKQ ANFTVDKHTQ HFRTKGEADA
     LDIDYELSFG GIPVPGKPGT FLKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYTVGNVTFS
     CSEPQIVPIT FVNSRRSYLL LPGTPQIDGL SVSFQFRTWN TDGLLLSTEL SEGSGTLLLS
     LEGGTLRLTI QKMANHAAEI LTGSKLNDGL WHSVSINARR SRITLTLDND AASPAQDTTP
     VQIYSGNSYY FGGCPDNLTD SQCLNPTKAF QGCMRLIFID NQPKDLISVQ QGSLGNFSDL
     HIDLCSIKDR CLPNYCEHGG SCSQSWTTFY CNCSDTGYMG ATCHNSLYKQ SCEVYRHQGN
     TAGFFYIDAD GSGPLGPLQV YCNITEDKIW TLVQHNNTEL TRVRGAGPEN PYVMALDYGS
     SMEQLEGVID GSEHCEQEVA YHCRRSRLLN TPDGTPFTWW IGRSNERHPY WGGSPPGVQQ
     CECGLDESCL DIRHFCNCDA DKDEWTNDTG FLSFKDHLPV TQIVITDTNR SNSEAAWRIG
     PLRCYGDRHF WNAVSFYTEA SYLHFPTFHA EFSADISFFF KTTALSGVFL ENLGIKDFIR
     LEISSPSEIT FSIDVGNGPV ELVVQSPSLL NDNQWHYVRA ERNLKETSLQ VDSLPRRVRE
     TSEEGHFRLQ LNSQLFVGGT SSRQKGFLGC IRSLHLNGQK LDLEERAKVT AGVRPGCPGH
     CSSYGSTCHN GGKCVEKHSG YFCDCTNSPY EGPFCKKEVS AVFKAGTSVT YMFQEPYPVT
     KNVSLSSSAI YVDAAPSKEN IAFSFMTAQA PSLLLYINSS SQDFLAVLLC KNGSLQVRYQ
     LSKEESHVFT IDVENFANRR IHRLKINREG RELTIQVDQQ LRLSYIFSPD VEFRALRSLT
     LGRVTENLGL DPEVAKANTL GFVGCLSSVQ YNHIAPLKAA LRHATIAPVT VQGTLTESSC
     GFMMDSDVNA VTTVHSSSDS FGKTDEREPL TNAVRSDSAV IGGVIAVVIF ITFCIVGIMT
     RFLYQHKQSH RTNQMKEKEY PDNLDGSFRN DIDLQHTVSE CKREYFI
//

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