ID   CAF1_EPHMU              Reviewed;         547 AA.
AC   P18856;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Collagen EMF1-alpha;
DE   AltName: Full=Fibrillar collagen;
DE   Flags: Precursor; Fragment;
GN   Name=COLF1;
OS   Ephydatia muelleri (Mueller's freshwater sponge) (Spongilla muelleri).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Spongillida; Spongillidae; Ephydatia.
OX   NCBI_TaxID=6052;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2395869; DOI=10.1073/pnas.87.17.6669;
RA   Exposito J.-Y., Garrone R.;
RT   "Characterization of a fibrillar collagen gene in sponges reveals the early
RT   evolutionary appearance of two collagen gene families.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6669-6673(1990).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA29119.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M34640; AAA29119.1; ALT_INIT; Genomic_DNA.
DR   PIR; A36046; A36046.
DR   AlphaFoldDB; P18856; -.
DR   SMR; P18856; -.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   SMART; SM00038; COLFI; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   3: Inferred from homology;
KW   Collagen; Extracellular matrix; Glycoprotein; Hydroxylation; Repeat;
KW   Secreted.
FT   CHAIN           <1..336
FT                   /note="Collagen EMF1-alpha"
FT                   /id="PRO_0000005710"
FT   PROPEP          337..547
FT                   /note="C-terminal propeptide"
FT                   /id="PRO_0000005711"
FT   DOMAIN          343..547
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          <1..280
FT                   /note="Triple-helical region"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..336
FT                   /note="Telopeptide"
FT   MOD_RES         187
FT                   /note="Allysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   547 AA;  53532 MW;  E384681A16141606 CRC64;
     GVPGPNGDVG PAGPTGPAGL DGAPGAQGPD GEPGLPGLPG QSGKSGASGQ PGVPGPVGAA
     GKPGSIRGQP GPPGPPGDLG RPGERGAKGV RGTPGAPGVD GVAGIAGAIG FPGPMGPDGA
     AGPSGYPGFD GVAGKPGPQG AMGPKGQAGE RGPQGTPGTQ GSKGVVGPKG VVGPQGDSGD
     TGDAGQKGAR GTAGSVGAKG TVGLPGNQGP QGPAGLKGVK GEKGEVGDKG ILGPDGDKGP
     TGMSGDAGPA GPIGDAGIQG PPGQDGPTGA QGPRGGQGPK GPAGAVGDVG DRGSTGPAGP
     PGPPGPTGGG IILVPVNDQN PTRSPVSGSV FYRGQAEETD VNLGSVADVI ELHKKLQHLK
     SPTGTKDSPA RSCHDLFLED NSTSDGYYWI DPNGGCIGDA VKVFCNFTGG VQQTCISATK
     NAGDLKSWSG HSIWFSDMLG GFKLTYDISR SQLQFIRAAS RHAVQSFTYK CRNSAAAVIF
     RTQDNKEIAA NKVTYDGCKS RPSVPDAAFV AVETKRVEQL PIRDFASSDI AGQHQEFGFE
     MGPACFY