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CSPL1_CHLAT
ID   CSPL1_CHLAT             Reviewed;         162 AA.
AC   P0DI72;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=CASP-like protein 0U1;
DE            Short=CaCASPL0U1;
OS   Chlorokybus atmophyticus (Soil alga).
OC   Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales;
OC   Chlorokybaceae; Chlorokybus.
OX   NCBI_TaxID=3144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. UTEX 2591;
RX   PubMed=22253761; DOI=10.1371/journal.pone.0029696;
RA   Timme R.E., Bachvaroff T.R., Delwiche C.F.;
RT   "Broad phylogenomic sampling and the sister lineage of land plants.";
RL   PLoS ONE 7:E29696-E29696(2012).
RN   [2]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=24920445; DOI=10.1104/pp.114.239137;
RA   Roppolo D., Boeckmann B., Pfister A., Boutet E., Rubio M.C.,
RA   Denervaud-Tendon V., Vermeer J.E., Gheyselinck J., Xenarios I., Geldner N.;
RT   "Functional and evolutionary analysis of the CASPARIAN STRIP MEMBRANE
RT   DOMAIN PROTEIN family.";
RL   Plant Physiol. 165:1709-1722(2014).
CC   -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC       family. {ECO:0000305}.
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DR   EMBL; HO417223; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; HO424356; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DI72; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008253; Marvel.
DR   Pfam; PF01284; MARVEL; 1.
DR   PROSITE; PS51225; MARVEL; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..162
FT                   /note="CASP-like protein 0U1"
FT                   /id="PRO_0000418714"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..43
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        162
FT                   /note="V -> G (in Ref. 1; HO424356)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   162 AA;  17565 MW;  5799438A88AE03A3 CRC64;
     MAAVEAAKTP RFILLIIEWV FALVAFAVMG HYLFDDRRSS FEYLTAICIL VWLVVMIYMV
     ILCCGRALPP LIEAAIFLLF AILVFIAFLV TAVKCNNSET IVIAGQTISR KVCEGESEPK
     AAAAFAFLLG LLLAGSSVLG CIAFRRPSAP PLSSFQNPTS SV
 
 
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