ID   A0A3Q1CPL8_AMPOC        Unreviewed;       979 AA.
AC   A0A3Q1CPL8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Collagen alpha-1(XXVIII) chain-like {ECO:0000313|Ensembl:ENSAOCP00000029922.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000029922.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000029922.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1CPL8; -.
DR   Ensembl; ENSAOCT00000024464.1; ENSAOCP00000029922.1; ENSAOCG00000020666.1.
DR   GeneTree; ENSGT00940000163195; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd22628; Kunitz_collagen_alpha1_XXVIII; 1.
DR   CDD; cd01450; vWFA_subfamily_ECM; 1.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24020:SF70; PH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF00092; VWA; 2.
DR   PRINTS; PR00759; BASICPTASE.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00327; VWA; 2.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF53300; vWA-like; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50234; VWFA; 2.
PE   4: Predicted;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT   DOMAIN          7..189
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          615..795
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          920..970
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          264..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..506
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  102728 MW;  98142316D54E85BE CRC64;
     DEDCSLELSF LVDSSESAKD NHEQEKRFVM NMVDRLQGVR LQTGRSLSLR VALLQYSSHV
     ITEQTFSEWR GSENFKTRIA PIIYIGHGTY TTYAITNMTK IYLEESSPGS VKVVVLLTDG
     ISHPRNPDIF SAVADAKNQG IKFFTLGITR TANEPANVAQ LRLLASSPTS HYLHNLQDED
     IVEKIATAIV SIMPCLSAEC TEKNFDALAV NKRHFAGERG PPGPPGIQGE TGVGLPGPKV
     RQTSPDNNIN MALFVCQISH SGLSLQGPQG PQGVQGEKGP HGEGFPGPKL YTLLTVVFYF
     QGELGPHGSP GPTGPVGAGI QGEKGTEGPR GPPGVRGLPG EGLPGPKGDQ GLPGEQGAPG
     ERGIGEPGPK GEPGAAGLSG LPGLPGEDGA PGQKGEPGLP GLRGPEGAQG IGAQGEKGDQ
     GPRGIRGLHG PPGISGPSGP KGERGVSGQQ GMPGQPGRSI SGPKGDVGSA GPPGPIGETG
     HGLPGPKVNP GPPGLPGLPG EPGPEGIGIP GPKGDVGFRG LPGLPGPPGE GLQGPPGEPG
     SQGMTGPRGP QGDGFPGAKG DRGLQGERGM KGTKGDLGDP GVPGEMGRNG AKGDPGLTYI
     IFSGCGIKCK ERPMELVFVI DSSESVGPEN FEIIKDFVTR LVDRTTVGHN ATRIGLVLYS
     LDVHLEFNLA RHRTKQDVKQ AIRKMPYMGE GTYTGTAIRK ATQEAFFGAR SGVRKVAIVI
     TDGQTDKREP VKLDIAVREA HAANIEMYAL GIVNSSDPTQ AEFLRELNLI ASDPDSEHMY
     LIDDFNTLPA LESKLVSQFC EDENGALIYN RVTNGHWNGN NGLNGNNGHG DNTNGYNGYG
     NNGYGYGNNG YGNNGNGYNY QEENQNLRRT NSRVRGDTFA LPISADDVVL SSSSSSSASS
     SSSSATSFSS PEAVPLDPRC NLSLDQGTCR DYSIRWYYDK QANSCAQFWY GGCGGNDNRY
     ETEDECKKTC VLLRTGNLC
//