ID L5KIF3_PTEAL Unreviewed; 1002 AA.
AC L5KIF3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Calsyntenin-1 {ECO:0000313|EMBL:ELK10546.1};
GN ORFNames=PAL_GLEAN10013024 {ECO:0000313|EMBL:ELK10546.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK10546.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004614}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004614}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00035006}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00035006}.
CC -!- SIMILARITY: Belongs to the CTNNBIP1 family.
CC {ECO:0000256|ARBA:ARBA00006505}.
CC -!- SIMILARITY: Belongs to the calsyntenin family.
CC {ECO:0000256|ARBA:ARBA00035015}.
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DR EMBL; KB030727; ELK10546.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KIF3; -.
DR STRING; 9402.L5KIF3; -.
DR eggNOG; KOG1834; Eukaryota.
DR InParanoid; L5KIF3; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR GO; GO:0042988; F:X11-like protein binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 2.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.10.10.490; Beta-catenin-interacting ICAT; 1.
DR Gene3D; 2.60.40.60; Cadherins; 2.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR026914; Calsyntenin.
DR InterPro; IPR045588; CLSTN_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR009428; ICAT_dom.
DR InterPro; IPR036911; ICAT_sf.
DR PANTHER; PTHR14139; CALSYNTENIN; 1.
DR PANTHER; PTHR14139:SF4; CALSYNTENIN-1; 1.
DR Pfam; PF00028; Cadherin; 1.
DR Pfam; PF19699; CLSTN_C; 1.
DR Pfam; PF06384; ICAT; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 2.
DR SUPFAM; SSF81730; beta-catenin-interacting protein ICAT; 1.
DR SUPFAM; SSF49313; Cadherin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS50268; CADHERIN_2; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PROSITE-ProRule:PRU00043};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..186
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 187..287
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 937..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..973
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 111467 MW; 0BB3D6A0056FACC1 CRC64;
MNREGAPGKS PEDVYVQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVASS QLSQLPQHPI
DQANKHKPWL EPTYHGIVTE NDDAVLLDPP LIALDKDAPL RFAGEICGFK IHGQNVPFDA
VVVDKSTGEG IIRSKEKLDC ELQKDYTFTI QAYDCGKGPD GASVKKSHKA TVHIQVSDVN
EYAPVFKEKS YKATVVEGKQ YESIVRVEAV DADCSPQFSQ ICSYEIVTPD APFTVDKDGY
IKNTEKLNYG KEHQYKLTVT AYDCGKKRAA EDVLVKISVK PTCTPGWQGW SSRVEYEPGT
GALALFPDIR LETCDESVAS VQVTVELETS HIGKGCDRDT YSEKSLHRLC GAASGTAELL
PSPSSSANWT VGLPTDNGHD SDQVFEFNGT QAVRVPDGLV SVSPKEPFTI SVWMRHGPFG
RKKETILCSS DRTDMNRHHY SLFVHGCRFV FLLRQDPSGE KKYKPAEFHW KLNQVCDEEW
HHYVLNVDIP RVTLYVDGVS HEPFSVTEDH PLHPSRTETQ LVVGACWQEY SGVESDNETE
PVPVASAGGD LRMTQFFRGD LAGLTIRSGK LADKKVIDCL YTCKEGLDLQ VPGDSGGGVK
IEANPSQSML TLEGEDVREL EKAVQHVAYL NSRQFPTPGI RRLKLSSTVR CFNEAACISV
PPVDGCVMVL QPEEPKISLS GVHHFARAAS EFESSEGVFL FPELRIISTI TREVEPDGEG
DEDPTVQESL VSEEVVHDLD TCEVTVEGEE LNPEWESLEV DVARLQHSGI EASSSGLGMT
FTGVDTMASY EEVLHLLRYR NWHSRSLLDR KFKLVCSELN GRYISNEFQV EVNVIHTASP
VEHASHMAAQ PQFVHPEHRS FVDLSGHNLA SPHPFAVVPS TATVVIVVCV SFLVFMIILG
VFRIRAAHQR TMRDQDAGKE NEMDWDDSAL TITVNPMETY EDQHSSEEEE EEEEEEESED
GEDDEVTSAE SESSEEEGGE HGDRQAVSRQ QQLEWDDSTL SY
//