ID   CSPL8_SORBI             Reviewed;         452 AA.
AC   C5XTX2;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=CASP-like protein 4A1;
DE            Short=SbCASPL4A1;
GN   OrderedLocusNames=Sb04g002820;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623;
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA   Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
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; CM000763; EES06244.1; -; Genomic_DNA.
DR   RefSeq; XP_002453268.1; XM_002453223.1.
DR   AlphaFoldDB; C5XTX2; -.
DR   STRING; 4558.Sb04g002820.1; -.
DR   EnsemblPlants; EES06244; EES06244; SORBI_3004G032500.
DR   GeneID; 8057526; -.
DR   Gramene; EES06244; EES06244; SORBI_3004G032500.
DR   KEGG; sbi:8057526; -.
DR   eggNOG; ENOG502QW75; Eukaryota.
DR   HOGENOM; CLU_048961_1_0_1; -.
DR   InParanoid; C5XTX2; -.
DR   OMA; SHTADPN; -.
DR   OrthoDB; 1502083at2759; -.
DR   Proteomes; UP000000768; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006702; CASP_dom.
DR   Pfam; PF04535; DUF588; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..452
FT                   /note="CASP-like protein 4A1"
FT                   /id="PRO_0000391522"
FT   TOPO_DOM        1..305
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..347
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        369..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        407..423
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..452
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..274
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  48348 MW;  ECF93E41AF8A7C2F CRC64;
     MGLRDSLKER EDRRSSEEEG DARQSWMTRE STTGWRKEST AALGTPVADW QCVLLLQFGA
     LQQKLLKAFP RAGPRPTTTL VPARPERARK KPHSQPPPST HMALQAQATA SPSPSPSPTR
     GRTGSGEWPD DAEKLPIAAT ASPARSSDAV ELVVVASTRH AAAAKYVPRR STSHTADPNP
     GRGGGGGSAG WYSWNGGRTR TAAPPRHARA DPPPAPPRRQ QPVEAPPPPP PPPPPPAPAP
     ALPPPVPPSP PAPAQAPVPP SATAPAPAPV PAPRASSPHV QFRSADQVVP NILSRKRRAA
     AMQRTALLAR GAAAGLCLAA LAVLAADTRK GWARDSYSNY TQFRYSEAVN VIGFIYSVFQ
     FVALVELMRR NKHLIPHPKR DLFDFTMDQV LTYLLISSSS SATARVSDLI DNWGSDPFPS
     MANGSIAISF LAFAVFAICS LISAYNLFRR DV