CO1A2_SCESX
ID CO1A2_SCESX Reviewed; 413 AA.
AC C0HLI6;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=Collagen alpha-2(I) chain {ECO:0000303|PubMed:31171860};
DE AltName: Full=Alpha-2 type I collagen {ECO:0000250|UniProtKB:P08123};
DE Flags: Fragments;
OS Scelidotherium sp. (strain SLP-2019) (South American ground sloth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Pilosa; Folivora; Mylodontidae; Scelidotherium;
OC unclassified Scelidotherium.
OX NCBI_TaxID=2546665 {ECO:0000303|PubMed:31171860};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Bone {ECO:0000303|PubMed:31171860};
RX PubMed=31171860; DOI=10.1038/s41559-019-0909-z;
RA Presslee S., Slater G.J., Pujos F., Forasiepi A.M., Fischer R., Molloy K.,
RA Mackie M., Olsen J.V., Kramarz A., Taglioretti M., Scaglia F., Lezcano M.,
RA Lanata J.L., Southon J., Feranec R., Bloch J., Hajduk A., Martin F.M.,
RA Salas Gismondi R., Reguero M., de Muizon C., Greenwood A., Chait B.T.,
RA Penkman K., Collins M., MacPhee R.D.E.;
RT "Palaeoproteomics resolves sloth relationships.";
RL Nat. Ecol. Evol. 3:1121-1130(2019).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen). {ECO:0000305}.
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted. Secreted, extracellular space.
CC Secreted, extracellular space, extracellular matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in bones. {ECO:0000269|PubMed:31171860}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC {ECO:0000250|UniProtKB:P08123}.
CC -!- MISCELLANEOUS: These protein fragments were extracted from an ancient
CC phalanx bone collected at Arroyo Del Moro in Argentina.
CC {ECO:0000269|PubMed:31171860}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family. {ECO:0000305}.
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DR AlphaFoldDB; C0HLI6; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 4.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Extinct organism protein; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Secreted.
FT CHAIN 1..413
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000448461"
FT REGION 1..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 10
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 21
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 27
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 82
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 313
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 316
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 82
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT UNSURE 6
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 14
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 78
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 102
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 151
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 170
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 188
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 197
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 206
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 216
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 270
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 279
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 318
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 324
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 342
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 386
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT UNSURE 407
FT /note="L or I"
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_CONS 12..13
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_CONS 53..54
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_CONS 61..62
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_CONS 82..83
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_CONS 159..160
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_CONS 210..211
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_CONS 378..379
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:31171860"
FT NON_TER 413
FT /evidence="ECO:0000303|PubMed:31171860"
SQ SEQUENCE 413 AA; 37111 MW; BD8184C4CA899B13 CRC64;
FDFSFLPQPP QEGLMGPRGP PGASGAPGPQ GFQGPAGEPG EPGQTGPAGA RGPGPPGKAG
EGVVGPQGAR GFPGTPGLPG FKGEPGAPGE NGTPGQTGAR GLPGERGRVG APGPAGSRGS
DGSVGPVGPA GPIGSAGPPG FPGAPGPKGE LGPVGNTGPG PAGPRGEQGL PGVSGPVGPP
GNPGANGLTG AKGAAGLPGV AGAPGLPGPR TGARGLVGEP GPAGSKGESG GKGEPGSAGP
QGPPGSSGEE GKRGPSGESG STGPTGPPGL RGGPGSRGLP GADGRAGVIG PAGARGASGP
AGVRGPSGDT GRPGEPGLMG ARGLPGSPGN VGPAGKEGPA GLPGIDGRPG PIGPAGARGE
AGNIGFPGPK GPAGDPGKGE KGHAGLAGNR GAPGPDGNNG AQGPPGLQGV QGG
