ID A0A1S3FI08_DIPOR Unreviewed; 1293 AA.
AC A0A1S3FI08;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Contactin-associated protein-like 5 isoform X2 {ECO:0000313|RefSeq:XP_012876136.1};
GN Name=Cntnap5 {ECO:0000313|RefSeq:XP_012876136.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012876136.1};
RN [1] {ECO:0000313|RefSeq:XP_012876136.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012876136.1};
RG RefSeq;
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 RefSeq; XP_012876136.1; XM_013020682.1.
DR GeneID; 105988917; -.
DR CTD; 129684; -.
DR OrthoDB; 4255614at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 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:UP000081671};
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..1293
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010373415"
FT TRANSMEM 1225..1250
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..360
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 367..544
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 546..583
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 582..634
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 778..943
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 944..982
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1007..1186
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 916..943
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1293 AA; 143953 MW; 8AA30EDD0A4E72E0 CRC64;
MDSTARLTSV LTLLFSGLWQ LGLTATNYNC DDPLASLLSP MAFSSSSDLT GTPISAQLNW
RVGTGGWSPA DSSAQQWLQM DLGNRVEITA VATQGRYGSS DWVTSYSLMF SDTGRNWKQY
KQEDSIWTFA GNMNADSVVH HKLLHSVRAR FIRFVPLEWN PSGKIGMRVE VYGCSYKSDV
ADFDGRSSLL YRFNQKLMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQNGRLAL
YLNLDDSKAR LSSSPPLATL GSLLDDQHWH SVLIERVGKQ VNFTVDKHTE HFRTKGEADA
LDIDYELSFG GIPVPGKPGT FLKKNFHGCI ENLYYNGINI IDLAKRRKHQ IYTGNVTFSC
SEPQIVPITF VNSSSSYLLL PGTPQIDGLS VSFQFRTWNK DGLLLSTELS EGSGTLLLSL
EGGILRLAIQ KTTQHVAEIL TGSSLNDGLW HSVSINARRS RITLTLDNDS ASPAQDTARV
QIYSGNSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGNFSDLH
IDLCSIKDRC LPNYCEHGGR CSQSWTTFYC NCSDTGYTGG TCHDSIYEQS CEVYRHQGNT
AGFFYVDPDG TGPLGPLQVY CNITEDKIWM SVQHNNTELT RVQGSSPEKP YTMTLDYGGS
MEQLEALIDG SEHCEQEVAY HCRRSRLLNT PDGTPFTWWI GRANERHPYW GGSLPGVQQC
ECGLEENCLD LTSDTGFLSF KDHLPVTQIV ITDTNRSNSE AAWRIGPLRC YGDRHFWNAV
SFYTEASYLH FPTFHAEFSA DISFFFKTTA LSGVFLENLG MKDFIRLEMS SPSEIMFAID
VGNGPVELIV QSPSLLNDNQ WHYIRAERNL KETSLQVDSL PRSTRQTSED GHFRLQLNSQ
LFVGGTSSRQ KGFVGCIRSL HLNGQKLDLE ERAKVTSGVR PGCPGHCSSY GSNCHNGGKC
VEKHSGYSCD CTNSPYEGPF CQKEVSAVFE ASASITYMFQ EPYPVTKNMS LSSSSIYTDV
TPSKEIIALS FVTAQAPSLL LFINSSSQDF LALYICKNGS LQVRYQLGKE ESYVFTIDAE
NFANRRMHHV KISREGRELT IQMDQQFRLS YNFSPEAEFR PVRSLTLGKI TENVGLDSEI
AKANTLGFVG CLSSVQYNHI APLKAALRHT TIAPVTVQGT LTESSCGAMV DSDVNAVTTV
HSSSDPFGKT DEREPLTNAV RSDSAVIGGV IAVVIFITFC IIGIMTRFLY QQKQTHRTNQ
MKEKEYPDNL DSSFRNDIDL QNTVSECKRE YFI
//
