ID   SSGP_VOLCA              Reviewed;         485 AA.
AC   P21997;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Sulfated surface glycoprotein 185;
DE            Short=SSG 185;
DE   Flags: Precursor;
OS   Volvox carteri (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=f. Nagariensis / HK10;
RX   PubMed=2689458; DOI=10.1083/jcb.109.6.3493;
RA   Ertl H., Mengele R., Wenzl S., Engel J., Sumper M.;
RT   "The extracellular matrix of Volvox carteri: molecular structure of the
RT   cellular compartment.";
RL   J. Cell Biol. 109:3493-3501(1989).
CC   -!- FUNCTION: The extracellular matrix (ECM) of Volvox contains insoluble
CC       fibrous layers that surround individual cells at a distance to form
CC       contiguous cellular compartments. SSG 185 is the monomeric precursor of
CC       this substructure (C3Z structure).
CC   -!- SUBUNIT: Polymer.
CC   -!- PTM: Intersubunit cross-links are formed between saccharide chains
CC       rather than between polypeptide chains.
CC   -!- PTM: Hydroxylated on proline residues in the Pro-rich central domain.
CC   -!- PTM: Glycosylated; contains sulfate-substituted glycans.
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DR   EMBL; X51616; CAA35953.1; -; mRNA.
DR   PIR; A33647; A33647.
DR   AlphaFoldDB; P21997; -.
DR   InterPro; IPR024616; Pherophorin.
DR   Pfam; PF12499; DUF3707; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydroxylation; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..485
FT                   /note="Sulfated surface glycoprotein 185"
FT                   /id="PRO_0000022421"
FT   REGION          212..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..317
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   485 AA;  50437 MW;  A52216400A031421 CRC64;
     MSKLLLVALF GAIAVVATSA EVLNLNGRSL LNNDDPNAFP YCKCTYRQRR SPYRLKYVGA
     ENNYKGNDWL CYSIVLDTTG TVCQTVPLTE PCCSADLYKI EFDVKPSCKG TVTRAMVFKG
     IDRTVGGVRV LESISTVGID DVTGVPGAAI LRIVKDLALP YSVVASFLPN GLPVCINRVP
     GSCTFPELFM DVNGTASYSV FNSDKDCCPT GLSGPNVNPI GPAPNNSPLP PSPQPTASSR
     PPSPPPSPRP PSPPPPSPSP PPPPPPPPPP PPPPPPSPPP PPPPPPPPPP PPPPPSPSPP
     RKPPSPSPPV PPPPSPPSVL PAATGFPFCE CVSRSPSSYP WRVTVANVSA VTISGGAGER
     VCLKISVDNA AAATCNNGLG GCCSDGLEKV ELFANGKCKG SILPFTLSNT AEIRSSFSWD
     STRPVLKFTR LGLTYAQGVA GGSLCFNIKG AGCTKFADLC PGRGCTVAVF NNPDNTCCPR
     VGTIA