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Database: UniProt
Entry: A0A286XJT1_CAVPO
LinkDB: A0A286XJT1_CAVPO
Original site: A0A286XJT1_CAVPO 
ID   A0A286XJT1_CAVPO        Unreviewed;       989 AA.
AC   A0A286XJT1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Calsyntenin 1 {ECO:0000313|Ensembl:ENSCPOP00000025573.1};
GN   Name=CLSTN1 {ECO:0000313|Ensembl:ENSCPOP00000025573.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000025573.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000025573.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000025573.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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 calsyntenin family.
CC       {ECO:0000256|ARBA:ARBA00035015}.
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DR   EMBL; AAKN02028894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A286XJT1; -.
DR   STRING; 10141.ENSCPOP00000025573; -.
DR   Ensembl; ENSCPOT00000037765.1; ENSCPOP00000025573.1; ENSCPOG00000010014.4.
DR   VEuPathDB; HostDB:ENSCPOG00000010014; -.
DR   GeneTree; ENSGT00950000183086; -.
DR   InParanoid; A0A286XJT1; -.
DR   OMA; IKVNRVC; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000010014; Expressed in frontal cortex and 13 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0098845; C:postsynaptic endosome; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR   GO; GO:0042988; F:X11-like protein binding; IEA:Ensembl.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; IEA:Ensembl.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0090128; P:regulation of synapse maturation; IEA:Ensembl.
DR   GO; GO:0099003; P:vesicle-mediated transport in synapse; IEA:Ensembl.
DR   CDD; cd11304; Cadherin_repeat; 2.
DR   Gene3D; 2.60.120.200; -; 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   PANTHER; PTHR14139; CALSYNTENIN; 1.
DR   PANTHER; PTHR14139:SF4; CALSYNTENIN-1; 1.
DR   Pfam; PF00028; Cadherin; 1.
DR   Pfam; PF19699; CLSTN_C; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
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:UP000005447};
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        868..888
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..172
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          173..273
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          922..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..966
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        971..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   989 AA;  109873 MW;  65BBEE92E10FBE27 CRC64;
     MAAAEAGPVP ELVPLQRTLG EKVRDTSPLK GSRHLQNLVN KHKPWLEPTY HGIVTENDNT
     VLLDPPLIAL DKDAPLRFAE SFEVTVTKEG EICGFKIHGQ NVPFDAVVVD KSTGEGIIRS
     KEKLDCELQK DYTFTIQAYD CGKGPDGAGV KKSHKATVHI QVNDVNEYAP VFKEKSYKAT
     ATEGKQHDSI LRVEAVDADC SPQFSQICSY EIVTPNVPFA VDKDGYIRNT EKLSYGKEQQ
     YKLSVTAYDC GKKRAAEDVL VKISIKPTCT PGWQGWSNRV EYEPGTGALA VFPNIHLETC
     DEPVALVQAT VELETSHIGK GCDRDTYSEK SLHRLCGAAA GTAELLPSPS SSLNWTIGLP
     TDNGHDSDQV FEFNGTQAVR IPDGVVSINP KEPFTISVWM RHGPFGRKKE TILCSSDKTD
     MNRHHYSLYV HGCRLIFLLR QDPSEEKRYR PAEFHWKLNQ VCDAEWHHFV LNVELPSATL
     YVDGVPHEPF SVTEDYPLHP SKIDTQLVVG ACWQEYSGVE SDNDTEPVTV ASAGGDLHMA
     QFFRGNLAGL TVRSGKLTDK KVIDCLYTCK EGLGLQGPED SGGVQIRAGP SQSVLTLEGD
     DIGELDRAMQ HLSYLNSRQF PTPGIRRLRV TSTAKCFNEA ATCIEIPVVE GYVMVLQPEE
     PKISLSGIHH FARAASEFES PEGVFLFPEL RIISTITREV EPEGDGAEDP TVQESLVSEE
     VVHDLDTCEV TVEGEELNPE QESLEVDAVR LQQKGIEVSH SDLGVVLRGV DTMASYEEVL
     HLLRYRNWHA SSLLDRKFKL ICSELNGRYL SNEFKVEVNV IHTASPVEHA SHMAAQPQFV
     HPEHRSFVDL SGHNLANPHP FAVVPSTATV VIVVCVSFLV FMIILGVFRI RAAHQRTMRD
     QDSGKENEMD WDDSALTITV NPMETYEDQH SSEEEEEEEE EEESEDGEEE EDITSAESES
     SEEEEGGPGD GQNATRQQQL EWDDSTLSY
//
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