SCAM_PEA
ID SCAM_PEA Reviewed; 289 AA.
AC Q9ZTX0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Secretory carrier-associated membrane protein;
DE Short=Secretory carrier membrane protein;
GN Name=PSAM2;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Root;
RX AGRICOLA=IND21960597; DOI=10.1006/pmpp.1998.0156;
RA Krajinski F., Martin-Laurent F., Gianinazzi S., Gianinazzi-Pearson V.,
RA Franken P.;
RT "Cloning and analysis of psam2, a gene from Pisum sativum L. regulated in
RT symbiotic arbuscular mycorrhiza and pathogenic root-fungus interactions.";
RL Physiol. Mol. Plant Pathol. 52:297-307(1998).
CC -!- FUNCTION: Probably involved in membrane trafficking. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- INDUCTION: Up-regulated in early interactions with pathogenic fingi and
CC down-regulated at late stages of mycorrhiza. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
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DR EMBL; AF018093; AAC82326.1; -; mRNA.
DR AlphaFoldDB; Q9ZTX0; -.
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:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Cytoplasmic vesicle; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..289
FT /note="Secretory carrier-associated membrane protein"
FT /id="PRO_0000304912"
FT TOPO_DOM 1..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 59..98
FT /evidence="ECO:0000255"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 32558 MW; BE992CFA9834B12B CRC64;
MAGRYDPNPF DEEQVNPFSN PRSAASATNS RPAPLNPDRA DYNYGFGPTV DIPLDTSTDG
KKKERDLQAK EAELRKREQE VRRKEEAIAR AGIVIEEKNW PPFFPIIHHD ITNEIPIHLR
TLQYVAFFSL LGLVLCLTWN VVSVTAAWIK GEGVKIWFLA IIYFIAGVPG AYALWYRPLY
RAFRTDSAIK FGWFFMFYLL HIGFCILAAV APPIVFKGKS LTGILSAIDV VGDYTLVGIF
YFIGFGFFCL ETLISIWVIQ QVYMHFRGGG KTAEMKREAA LGAMGAALR
