ID   COA_ACRMI               Reviewed;         888 AA.
AC   B8V7R6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Collagen alpha chain;
DE   Flags: Fragment;
OS   Acropora millepora (Staghorn coral) (Heteropora millepora).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Acroporidae; Acropora.
OX   NCBI_TaxID=45264;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=22490231; DOI=10.1111/j.1365-294x.2012.05554.x;
RA   Moya A., Huisman L., Ball E.E., Hayward D.C., Grasso L.C., Chua C.M.,
RA   Woo H.N., Gattuso J.P., Foret S., Miller D.J.;
RT   "Whole transcriptome analysis of the coral Acropora millepora reveals
RT   complex responses to CO(2)-driven acidification during the initiation of
RT   calcification.";
RL   Mol. Ecol. 21:2440-2454(2012).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 854-870, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=23765379; DOI=10.1093/molbev/mst109;
RA   Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA   Guichard N., Miller D.J., Marin F.;
RT   "The skeletal proteome of the coral Acropora millepora: the evolution of
RT   calcification by co-option and domain shuffling.";
RL   Mol. Biol. Evol. 30:2099-2112(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23765379}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble organic matrix of
CC       the aragonitic skeleton (at protein level).
CC       {ECO:0000269|PubMed:23765379}.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR   EMBL; JR991083; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; JR996633; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B8V7R6; -.
DR   SMR; B8V7R6; -.
DR   PRIDE; B8V7R6; -.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 4.
DR   SMART; SM00038; COLFI; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   1: Evidence at protein level;
KW   Collagen; Direct protein sequencing; Disulfide bond; Repeat; Secreted.
FT   CHAIN           <1..888
FT                   /note="Collagen alpha chain"
FT                   /id="PRO_0000429494"
FT   DOMAIN          3..60
FT                   /note="Collagen-like 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          513..571
FT                   /note="Collagen-like 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          661..884
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          1..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..255
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..623
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        691
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        723
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        731..882
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        793..833
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   888 AA;  87554 MW;  4FB8FC42C5FDCC40 CRC64;
     APGPDGLTGT KGSMGEPGTD GEPGSPGPQG AKGETGLAGR RGLTGIPGKQ GRQGERGEPG
     TAGSQGQQGQ PGTQGPPGLP GKQGETGEPG ESGEDGTPGP RGERGAQGER GATGMMGPSG
     DPGEAGIPGA DGKAGERGVP GAPGPVGTPG LPGMPGQQGP MGPIGAKGSK GDVGPTGERG
     YDGKDGEPGR DGSPGPIGQP GIPGEKGEDG VPGSDGTPGS RGDSGPRGLP GNPGPPGRPG
     ALGPSGPPGP QGPRGPRGEP GMKGPAGPPG RPGATGALGQ LGKTGLKGEP GNQGRRGPPG
     LQGDPGKPGQ SGPPGPPGPS GPSGRDGSDG QKGSSGEPGR PGKDGIPGQP GSNGKDGEPG
     TPGSDGRAGE IGPSGPIGPK GERGTPGATG PMGNSGPPGV QGSKGEKGPP GTNGRNGSPG
     ISGSRGAQGP PGAPGSSGQN GVDGGTGENG TNGRPGLKGE SGAPGDPGAS GSAGPAGPPG
     PKGDTGPPGI QGEKGRRGAD GIPGKTGEPG PQGDQGPKGQ KGEVGPVGEK GDKGWTGTPG
     DPGPQGDRGE PGPPGRDGVD GPPGPRGAPG EMGAVGDPGL NGSMGEPGNK GPDGDLGESG
     AKGPDGIKGP PGPPGPPGPP GQPGMSEIAS YLSVGNLEKG PGFRLYSSSG EEMPKQKIKA
     ENVLKDLDEK DKEMDSLIAP DGSRKFPAKT CYDLFLDHGN FESGEYWIDP NGGTVKDAIK
     VYCDKKKNSS CVYPTNPKIS DLVLKSGFES KEDKWLSKAF KKSEEVEYDA HYTQINFLRT
     LSNYANQNVT YACRNSKAWE DGQHSIKLMG SNDMEYHASS KISLRPTVIM NECANGGKLD
     KWGKTVLEID TRERSRLPIV DVSAFDVGRE GQDFKLEIGP ACFHHIKY