ID   CSPLE_PHYPA             Reviewed;         215 AA.
AC   A9SG36;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=CASP-like protein UU3;
DE            Short=PpCASPLUU3;
GN   ORFNames=PHYPADRAFT_233235;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Gransden 2004; TISSUE=Sporophyte;
RA   Kohara Y., Shin-i T., Nishiyama T., Suzuki Y., Sugano S., Hiwatashi Y.,
RA   Hasebe M.;
RT   "Expressed genes in Physcomitrella patens.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=DC950607; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=EDQ69824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS544964; EDQ69824.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DC950607; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_001765361.1; XM_001765309.1.
DR   AlphaFoldDB; A9SG36; -.
DR   EnsemblPlants; Pp3c7_13960V3.1; Pp3c7_13960V3.1; Pp3c7_13960.
DR   EnsemblPlants; Pp3c7_13960V3.2; Pp3c7_13960V3.2; Pp3c7_13960.
DR   Gramene; Pp3c7_13960V3.1; Pp3c7_13960V3.1; Pp3c7_13960.
DR   Gramene; Pp3c7_13960V3.2; Pp3c7_13960V3.2; Pp3c7_13960.
DR   HOGENOM; CLU_1285154_0_0_1; -.
DR   InParanoid; A9SG36; -.
DR   OMA; NGVSWED; -.
DR   Proteomes; UP000006727; Chromosome 7.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006459; CASP/CASPL.
DR   InterPro; IPR006702; CASP_dom.
DR   Pfam; PF04535; DUF588; 1.
DR   TIGRFAMs; TIGR01569; A_tha_TIGR01569; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..215
FT                   /note="CASP-like protein UU3"
FT                   /id="PRO_0000418672"
FT   TOPO_DOM        1..44
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..93
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   215 AA;  23051 MW;  E6F3148DCD792A7D CRC64;
     MATAWESEYF DKVTPGERER AVPPMVPQQT PPPVYIQPQV SRNGIVASIV LRLLTLIFAV
     VALAVLASNT GSFQVSTGSA TSVKTIKFTI LSAFTYLFAV CGVVAVYSLL LIIVEMIDLA
     VRGFTTHTLV AIFVFVLDQT MAYVLISAAS ASANGVKVSR DESNITGYKF DISCSNLGID
     DYCTKASASV AIAFIAFLFM AITAGVSARR LFKLP