ID   CSPL3_HORVV             Reviewed;         221 AA.
AC   F2E2E4;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=CASP-like protein 4B1;
DE            Short=HvCASPL4B1;
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Haruna Nijo; TISSUE=Seedling root, and Seedling shoot;
RX   PubMed=21415278; DOI=10.1104/pp.110.171579;
RA   Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA   Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA   Sato K.;
RT   "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT   from 12 clone libraries.";
RL   Plant Physiol. 156:20-28(2011).
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; AK370315; BAK01516.1; -; mRNA.
DR   AlphaFoldDB; F2E2E4; -.
DR   PRIDE; F2E2E4; -.
DR   Proteomes; UP000011116; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   InterPro; IPR006702; CASP_dom.
DR   Pfam; PF04535; DUF588; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..221
FT                   /note="CASP-like protein 4B1"
FT                   /id="PRO_0000417770"
FT   TOPO_DOM        1..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..125
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   221 AA;  23232 MW;  31CE7048AE049D53 CRC64;
     MAMQLHAASP DSEHYVAKSP PPPPPLSPHP EPAPAFVKPK SPHVSQGGNA PVATATTPLT
     PGRVDRARHD HHGGGGGGDE ATQLLNGIVL VLRAGAALLS FVAMALVASC RHGDWMDFLR
     YQEYRYLLGV SVVAFVYSAA QALKNFRRRR RGAADASFLD FAGDQAVAYL LVTASAAALP
     ITIRMRSAVV NVFTDAIAAS IALGFLAFAA LALSAMLSRH A