CSCL1_CAPHI
ID CSCL1_CAPHI Reviewed; 803 AA.
AC A0A452G813;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=CSC1-like protein 1;
DE AltName: Full=Transmembrane protein 63A;
GN Name=TMEM63A;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION (MICROBIAL FUNCTION), SUBCELLULAR LOCATION, AND INTERACTION WITH
RP H.CONTORTUS GAL-1.
RX PubMed=25879191; DOI=10.1186/s13071-015-0816-3;
RA Yuan C., Zhang H., Wang W., Li Y., Yan R., Xu L., Song X., Li X.;
RT "Transmembrane protein 63A is a partner protein of Haemonchus contortus
RT galectin in the regulation of goat peripheral blood mononuclear cells.";
RL Parasit. Vectors 8:211-211(2015).
RN [3]
RP INTERACTION WITH H.CONTORTUS GAL-1.
RX PubMed=28870237; DOI=10.1186/s13071-017-2353-8;
RA Lu M., Tian X., Yang X., Yuan C., Ehsan M., Liu X., Yan R., Xu L., Song X.,
RA Li X.;
RT "The N- and C-terminal carbohydrate recognition domains of Haemonchus
RT contortus galectin bind to distinct receptors of goat PBMC and contribute
RT differently to its immunomodulatory functions in host-parasite
RT interactions.";
RL Parasit. Vectors 10:409-409(2017).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel (By
CC similarity). Mechanosensitive ion channel that converts mechanical
CC stimuli into a flow of ion (By similarity).
CC {ECO:0000250|UniProtKB:Q91YT8}.
CC -!- FUNCTION: (Microbial infection) Involved in the immunomodulatory
CC effects exerted by H.contortus GAL-1 on host peripheral blood
CC mononuclear cells to down-regulate host immune response.
CC {ECO:0000269|PubMed:25879191}.
CC -!- SUBUNIT: (Microbial infection) Interacts with H.contortus GAL-1 (via
CC domain galectin 1). {ECO:0000269|PubMed:25879191,
CC ECO:0000269|PubMed:28870237}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O94886};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:25879191}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR EMBL; LWLT01000016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452G813; -.
DR STRING; 9925.ENSCHIP00000032717; -.
DR OMA; TQVIWSN; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:1990760; F:osmolarity-sensing cation channel activity; ISS:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0032944; P:regulation of mononuclear cell proliferation; IMP:UniProtKB.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027815; PHM7_cyt.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR003864; RSN1_7TM.
DR InterPro; IPR026957; TMEM63A.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR PANTHER; PTHR13018:SF24; PTHR13018:SF24; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Ion channel; Ion transport; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..803
FT /note="CSC1-like protein 1"
FT /id="PRO_0000448963"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 803 AA; 91821 MW; D5DAFED76BA88CFC CRC64;
MTDSPFLELW QSRTVAIRER LGIGDQPNDS YCYNSAKNST VLQGVTFGGI PTVLFIDVSC
FLFLIVVFSI IRRKFWDYGR IALVSEGNSE SRFRRLSSSS SGQQDFESEL GCCSWLTAIF
RLHDDQILEW CGEDAIHYLS FQRHIIFLLV VVSCLSLCII LPVNLSGDLL DKDPYSFGRT
TIANLQTDNN LLWLHTIFAI LYLILTVVFM RHHTQSIKYK EESLVRRTLF VTGLPKDAKK
ETVESHFRDA YPTCEVVEVQ LCYNVAKLIY LCKERKKTEK SLTYYTNLQV KTGQRTFINP
KPCGQFCCCE VRGCEWEDAI SYYTRMKDRL MERITEEECR VQDQPLGMAF VTFQEKSMAT
YILKDFNACK CQGLQCKGEP QPSSHSRELG ISRWSVTFAA YPEDICWKNL SIQGFRWWFQ
WLGINFILFV GLFFLTTPSI ILSTMDKFNV TKPIHALNDP IISQFFPTLL LWSFSALLPT
IVCYSTLLES HWTKSGENRI MMTKVYIFLI FMVLILPSLG LTSLDFFFRW LFDKTSSEAS
IRLECVFLPD QGAFFVNYVI ASAFIGNGME LLRLPGLILY TFRMVMAKTA ADRRNVKQHQ
AFEYEFGAMY AWMLCVFTVI MAYSITCPII VPFGLIYILL KHMVDRHNLY FAYLPAKLEK
RIHFAAVNQA LAAPILCLFW LYFFSFLRLG LKAPLTLFTF LVLLLTILVC LAYTCFGCFR
HLSPLNYKTE ESANDKGNEA GAHVPPPFTP YVPRILNSSS SEKTALSPQQ QTYGAINNIS
GTVAGQGLAQ SPEDSVAAAD QED
