PM27_STRPU
ID PM27_STRPU Reviewed; 267 AA.
AC Q26616;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=27 kDa primary mesenchyme-specific spicule protein;
DE Flags: Precursor;
GN Name=PM27;
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].
RX PubMed=7537234; DOI=10.1006/dbio.1995.1101;
RA Harkey M.A., Klueg K., Sheppard P., Raff R.A.;
RT "Structure, expression, and extracellular targeting of PM27, a skeletal
RT protein associated specifically with growth of the sea urchin larval
RT spicule.";
RL Dev. Biol. 168:549-566(1995).
CC -!- FUNCTION: May play a role in the regulation or execution of skeletal
CC growth.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted to the skeletal
CC compartment and accumulates predominantly at the advancing mineralizing
CC surface of the spicule tips. As the spicules elongate PM27 protein
CC disappears from the more mature mid-shaft regions. May be concentrated
CC at the mineral-nonmineral interface, rather than within the spicule
CC matrix.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the micromere/primary
CC mesenchyme cells (PMC) lineage. Produced uniformly and exclusively by
CC PMCs through the early prism stage and this specificity is further
CC restricted during skeletogenesis to a subpopulation of PMCs associated
CC with the growing tips of the spicules.
CC -!- DEVELOPMENTAL STAGE: Appears at the mesenchyme blastula stage.
CC -!- DOMAIN: The repetitive domain may provide a calcite binding matrix.
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DR EMBL; U18132; AAA85689.1; -; Genomic_DNA.
DR RefSeq; NP_999630.1; NM_214465.1.
DR AlphaFoldDB; Q26616; -.
DR SMR; Q26616; -.
DR EnsemblMetazoa; NM_214465; NP_999630; GeneID_373181.
DR GeneID; 373181; -.
DR KEGG; spu:373181; -.
DR CTD; 373181; -.
DR HOGENOM; CLU_1754377_0_0_1; -.
DR InParanoid; Q26616; -.
DR OMA; QGPGMRP; -.
DR PhylomeDB; Q26616; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..267
FT /note="27 kDa primary mesenchyme-specific spicule protein"
FT /id="PRO_0000017564"
FT REPEAT 21..24
FT /note="1"
FT REPEAT 25..28
FT /note="2"
FT REPEAT 29..32
FT /note="3"
FT REPEAT 33..36
FT /note="4"
FT REPEAT 37..40
FT /note="5"
FT REPEAT 41..44
FT /note="6"
FT REPEAT 45..48
FT /note="7"
FT REPEAT 49..52
FT /note="8"
FT REPEAT 53..56
FT /note="9"
FT REPEAT 57..60
FT /note="10"
FT REPEAT 61..64
FT /note="11"
FT DOMAIN 79..220
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 20..64
FT /note="11 X 4 AA tandem repeats of G-[PQ]-G-[MQ]"
FT REGION 44..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 100..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 197..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 267 AA; 28580 MW; 2AC398C630DE5E07 CRC64;
MKLLAILLVL PALCFGQRHE GPGMGPGMGP GMGPGMGPGM GPGMGPGMGP GMGPGQGQGQ
GQGQGQVGGS KCKGGWFLIG QQCFKMMSRA LKWNDAELMC EQNAPCGTPV LGGVMTIPDI
QTSNAVINHL KSLSSTAMAI DIPFWTGLHN KWNALLERYE GWKWPAGWST TQQPLRFVNW
APREPNNQLL DQQHSYCARM NRMGQWYVVR CDEPMYFACS MPVSPPLVGG ANTNPGMGML
VENPAPIING YTEFESGLLM RNGVGGP