M130_STRPU
ID M130_STRPU Reviewed; 779 AA.
AC P08472;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Mesenchyme-specific cell surface glycoprotein;
DE AltName: Full=MSP130;
DE Flags: Precursor;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2295637; DOI=10.1016/s0021-9258(19)40029-x;
RA Parr B.A., Parks A.L., Raff R.A.;
RT "Promoter structure and protein sequence of msp130, a lipid-anchored sea
RT urchin glycoprotein.";
RL J. Biol. Chem. 265:1408-1413(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 542-779.
RX PubMed=3569664; DOI=10.1016/0012-1606(87)90135-7;
RA Leaf D.S., Anstrom J.A., Chin J.E., Harkey M.A., Showman R.M., Raff R.A.;
RT "Antibodies to a fusion protein identify a cDNA clone encoding msp130, a
RT primary mesenchyme-specific cell surface protein of the sea urchin
RT embryo.";
RL Dev. Biol. 121:29-40(1987).
CC -!- FUNCTION: Not known. Could be involved in mesenchyme cell migration,
CC adhesion, fusion, or spicule formation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Restricted to the primary mesenchyme cell lineage.
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DR EMBL; M31750; AAA30065.1; -; Genomic_DNA.
DR EMBL; M31751; AAA30066.1; -; mRNA.
DR EMBL; M16457; AAA30064.1; -; mRNA.
DR PIR; A35006; A35006.
DR AlphaFoldDB; P08472; -.
DR eggNOG; ENOG502S02S; Eukaryota.
DR HOGENOM; CLU_336276_0_0_1; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..779
FT /note="Mesenchyme-specific cell surface glycoprotein"
FT /id="PRO_0000021631"
FT REGION 249..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 779 AA; 81006 MW; 7D522D8348928316 CRC64;
MQFGVPLLVL CLALGSTEAT ISLKLVSRLY LPFDKLPVGG GAGGAGGAGG AGGGGGGGGG
AGGRGGGGGG RGQTGGMYAL NNGVAFKSAY DMDKQLAYVG GGQFVQIVDF SDVVQPKVVK
QIATEGPVAD IAECGDLVAF TQPGKPHFTD VGSLKIYEKY NPATMMMKEL CSVEVGSQPI
AVRFAQGCSL IIVANEGVMG ENNYTKKYVN PEGTITTVRL AGSVSNGPSQ QIVNTTFGAG
GPMMTTPMAG FPRGTTWSPN AGAGGQGGQG QYPGQGGQGG QGGQGGQGQY PGQGGQGGQG
GQGGQGGQGG YPGQGGQGGP GYYPGQGGQG GQGGQGGWGQ GGGQGGQGGG NNPQYPMIPT
TPLPGTICNG TSTMSYVVSQ INFHKFNAPA EVQRLKALHV RQPYTGQLGD PGPHTFSRGL
EPRHITLDQQ EQIAYISLQE NNAIAVVDLN NNTVIDILPM GVKNWKGLKI DASSADRGIL
FQTYDQLNSF PMPDAIETYY DAMGDLYVVT ANEGAKPMMA QCSLEVCPGG PGEFEEVEIG
EEFIVEELLP QPVIDSPLGQ AMAEETQLGS SLFSMVDGIN PAEPEFFNEV FMFGGRGISA
YKVDPITMNM TLAWDSGDVI EKEIAKFFPK IFNGAAFSRP PQRVKPFMTK DSRSSGRGPE
CESLAVGDVQ GRKLIFVGID GVSALAIFSV APGNSTPVYE SLFKDGHIDA SYNALYKNRK
TGRVSGTVSM YEVIDVPYWM LLKTLGTNIE GSSAISMTSS AFSIFFAFLS GMFAIFMKM