CSPLD_PHYPA
ID CSPLD_PHYPA Reviewed; 373 AA.
AC A9RZ57;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=CASP-like protein UU6;
DE Short=PpCASPLUU6;
GN ORFNames=PHYPADRAFT_161913;
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 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; DS544926; EDQ75777.1; -; Genomic_DNA.
DR RefSeq; XP_001759475.1; XM_001759423.1.
DR AlphaFoldDB; A9RZ57; -.
DR PRIDE; A9RZ57; -.
DR EnsemblPlants; Pp3c13_22040V3.1; Pp3c13_22040V3.1; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.11; Pp3c13_22040V3.11; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.12; Pp3c13_22040V3.12; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.2; Pp3c13_22040V3.2; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.3; Pp3c13_22040V3.3; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.4; Pp3c13_22040V3.4; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.5; Pp3c13_22040V3.5; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.6; Pp3c13_22040V3.6; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.7; Pp3c13_22040V3.7; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.8; Pp3c13_22040V3.8; Pp3c13_22040.
DR EnsemblPlants; Pp3c13_22040V3.9; Pp3c13_22040V3.9; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.1; Pp3c13_22040V3.1; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.11; Pp3c13_22040V3.11; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.12; Pp3c13_22040V3.12; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.2; Pp3c13_22040V3.2; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.3; Pp3c13_22040V3.3; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.4; Pp3c13_22040V3.4; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.5; Pp3c13_22040V3.5; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.6; Pp3c13_22040V3.6; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.7; Pp3c13_22040V3.7; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.8; Pp3c13_22040V3.8; Pp3c13_22040.
DR Gramene; Pp3c13_22040V3.9; Pp3c13_22040V3.9; Pp3c13_22040.
DR InParanoid; A9RZ57; -.
DR OrthoDB; 1502083at2759; -.
DR Proteomes; UP000006727; Chromosome 13.
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..373
FT /note="CASP-like protein UU6"
FT /id="PRO_0000391563"
FT TOPO_DOM 1..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 373 AA; 40318 MW; 2A17A59FD7B63035 CRC64;
MGTLTDPTVD PADPHVKADD GAGLIDAGQV HPERLETLAE DQSQRDGANG VHFPVKTNTG
NAAESTASTE NGETGSIDVG KLRTKPSPVQ THIHRGGSEG LYRGASGGIY RSASGSTHIH
RGASGGILRG QSGGIHRGRS GAIHLPSLQS ISFSMTRLPE EDAGVMMHFT ETKETETTPE
SSRASDEDAP TPKKKHRLRK HLTAIGAYSF AFRFSETVLS LIAIVVMCST RGSMRTDGVD
FGTLKFNHFQ AYRYLVAVNV IVFVYSTFQF IQLLYTVILG ISFIPSIFIS TWMTFGFDQL
FLYLLLSAST SAATVANMSY TGEMGIQLCS RFDVGSFCSK ADVAVTMSFF AVLAMLSSTI
LAIYRIAVLL REY
