ID A0A9J7HRC4_BRAFL Unreviewed; 1337 AA.
AC A0A9J7HRC4;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Collagen alpha-1(I) chain-like isoform X13 {ECO:0000313|RefSeq:XP_035662027.1};
GN Name=LOC118406220 {ECO:0000313|RefSeq:XP_035662027.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554, ECO:0000313|RefSeq:XP_035662027.1};
RN [1] {ECO:0000313|Proteomes:UP000001554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|Proteomes:UP000001554};
RX PubMed=32313176;
RA Simakov O., Marletaz F., Yue J.X., O'Connell B., Jenkins J., Brandt A.,
RA Calef R., Tung C.H., Huang T.K., Schmutz J., Satoh N., Yu J.K.,
RA Putnam N.H., Green R.E., Rokhsar D.S.;
RT "Deeply conserved synteny resolves early events in vertebrate evolution.";
RL Nat. Ecol. Evol. 0:0-0(2020).
RN [2] {ECO:0000313|RefSeq:XP_035662027.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035662027.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035662027.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR RefSeq; XP_035662027.1; XM_035806134.1.
DR GeneID; 118406220; -.
DR Proteomes; UP000001554; Chromosome 18.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR37456:SF5; COLLAGEN TYPE XIII ALPHA 1 CHAIN; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1337
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039950397"
FT DOMAIN 40..234
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 236..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..273
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..341
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..433
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..536
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..593
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..715
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..907
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1337 AA; 133223 MW; 0C6A7948C47FEF41 CRC64;
MMCLFAGEQG RLVCLLALVA VIATPGHGQE IIGESGGQQD IDLLQMIGVP LPTPIRFVSG
YDGFPAFEFG SEANIGRLAR TFFPNMFYKD FSILVTTRPN FQEGGILFAV TNSFQTVIQL
GLKIADAGKG RSGEALQNIT FIYTDTRNSE VTQEVARFTI PTTAGEWLRF SLSVRGNAVT
LYYDCEERET QFFDRTVSQL EFAPAAAVFV GQAGAAEEGK YLGSIQELLI RKDPNAAEQQ
CSGDAGEEGT VSGSGDGGEE GTIITIPGTV IPGRPNTPLA TQETPVDGPD VNEPYPDTSN
MERHDGDTTG WPELPEGGAN TGLAGLPGLP GVPGPKGDTG PQGPPGPRGE KGEPGDTTLV
EGPIGIPGDP GLPGLPGPKG DTGPVGPPGE RGLQGERGEA GLKGDPGVGL TGPPGPPGPP
GVVTVGDTGE PGESIAGVAG PPGPPGPPGL PGPPGPSNGF VPETGVAGPP GPPGPPGIPG
LPGPPGLPGL PGKPGTFGTG NITNGIQGPP GRDGVDGSAG PPGIPGIPGQ DGPIGPKGEA
GVPGIEGPAG TKGEPGLTGA PGLPGPPGPP GPSGGGGGIF GFGGSSGGPG PAGEPGIPGN
PGQKGEQGTA GPEGPQGTPG LPGPVGPRGQ KGDPGEAGIV GPQGPKGDMG PRGPAGEAGR
DGVGLPGPPG PPGPPGLPGT ISVLPGDDEM TVSPGFRPTG GEGEMTGGFP GGLIGPAGPE
GPRGPPGIAG PPGPIGRPGD DGAPGLKGDR GDSGEAGRKG DRGEPGPAVT VDGDVLQIKG
SKGEPGLDGV EGLPGIKGEP GEAGIQGPEG PIGPKGMIGE VGFPGRMGLP GVRGQKGEKG
DTGTGLPGPP GPPGPPGLPS GASFPAGSFP VLQKGEKGDI GPSGPPGPPG ALASGPGLSF
GGAGLVGPAG PKGEKGMMGI RGPLGRQGRK GEIGLPGRKG DRGEAGPPGA PGGFFGGSGQ
VVQGPTGPPG PQGPRGPPGF PGRGPSGPPG PRGPAGPAGI GAPGLPGPPG RPGQPGASIG
SGIMGPPGPP GPPGRAAGIV TFNSESHLLR SPPSSPGTLA FVADTEQLYL RVGGGWQIIL
TQPLRPTVQV GKIMSIPERP PVQPEASAEN PGHANNGFNN GFFGSEVDAP TVQLVGSPDS
NLGKATGKRL HLIALNEPMT GNMYGIRGAD FKCFQQARQA GLRGTFRAFL SSKVQDLSSV
VSRGDRDGIP IVNLKDEILF PSWNSIFEGE RETNEYKGGA FDINTAIYTF NGTQPLLNPT
WPHKRIWHGT NMDGQRLGDH FCNAWRENDV SFVGMASSLQ TGMLLGQEQY SCSSSYIVLC
IENTHKRHHR VYNYRRK
//
