ID   A0A3B4U412_SERDU        Unreviewed;      1038 AA.
AC   A0A3B4U412;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Collagen alpha-1(XXVIII) chain-like {ECO:0000313|Ensembl:ENSSDUP00000012625.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000012625.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000012625.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4U412; -.
DR   STRING; 41447.ENSSDUP00000012625; -.
DR   Ensembl; ENSSDUT00000012850.1; ENSSDUP00000012625.1; ENSSDUG00000009149.1.
DR   GeneTree; ENSGT00940000163195; -.
DR   OMA; VGPENYE; -.
DR   Proteomes; UP000261420; 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:SF18; COLLAGEN ALPHA-1(VI) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 3.
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   Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT   DOMAIN          85..267
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          670..850
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          977..1027
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          276..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          901..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1038 AA;  110584 MW;  941B275E357A4C6A CRC64;
     MSEPLFFFSF FLNPSLLSLY LLKGVMVPSL HWLLLLWGLQ GLCAQDYEED YEEEVVTTKK
     KNKLYPSNSI PQNGKSLIDE DCGLEIAFLI DSSESAKDNH AQEKRFASDV MDRLQGLRLQ
     TGRSLSSRAA LLQYSSHVII EQTFKQWRGT NDFKARIAPI VYIGHGTYTT YAITNLTRIY
     LEESNPSSIK VAVLLFDGIS HPRNPDIFSA VADAKNQGVR FFTIGITPEA NEPTNIAQLR
     LIASSPASRY LHNLQDRGIV EKIIKEICPL AQSKCACDKG ERGPSGPPGK KGRPGDDGSP
     GSKGQKGESG LSGLPGREGG EGDVGFQGQP GPPGPQGLGE PGSPVSIRSQ HTLFGERGLE
     GPRGPRGQPG TGIKGDKVEY REGVNKLPDC YCICLSLQGI EGPRGPPGSR GPPGEGLSGS
     KGDQGLPGEI GAPGERGAGD PGAKGEPGST GMAGLPGLPG EDGAPGQKGE PGATGFRGPE
     GAPGIGTQGE KGDQGQRGIR GLTGPPGIAG PSGPKVRIHQ AAGDLGPNGP PGPIGETGYG
     LPGPKVMLSM NKQCALYNSR VIRVLDVRLS THTHTHTQKS SISKREHHTV LPCLIQGEQG
     SQGVTGPRGL PGEGFPGAKG DRGSAGERGL KGIKGDMGDA GTPGQPREDI IRMIKEICGC
     GIKCKERPME LVFVIDSSES VGPENFEIIK DFVNALVDRV TVGRNATRIG LVLYSLEVKL
     VFNLARYVSK QDIKQAIRNI PYMGEGTYTG TAIRKATQEA FYSSRVGVSK VAIVITDGQT
     DKREPVKLDI AVREAHAANI EMFALGIVNT SDPTQAEFLR ELNLIASDPD SEHMFLIDDF
     NTLPALESKL VSQFCEDENG ALIYNRITNG YNGYRNGVNG HYAIGGYGYR PATEQEILNG
     RQTGTNTGAS THSHGGQVET TQHGSKGPVP PSREDSSGSR GSSSSSSSSS SSSSSSSSSS
     TNTTTSFSET VPLDPRCGLV LDQGTCRDYN IRWYYDKQAN ACAQFWYGGC NGNKNRFDTE
     EECKRTCVIT RSTGSTRS
//