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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
 
 
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