ID A0A7M7GRF4_APIME Unreviewed; 1173 AA.
AC A0A7M7GRF4; A0A8B6YZN2;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(IX) chain isoform X2 {ECO:0000313|RefSeq:XP_006564398.1};
GN Name=LOC412865 {ECO:0000313|RefSeq:XP_006564398.1};
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7460 {ECO:0000313|EnsemblMetazoa:XP_006564398};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_006564398}
RP IDENTIFICATION.
RC STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:XP_006564398};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_006564398.1}
RP IDENTIFICATION.
RC STRAIN=DH4 {ECO:0000313|RefSeq:XP_006564398.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_006564398.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
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DR RefSeq; XP_006564398.1; XM_006564335.3.
DR AlphaFoldDB; A0A7M7GRF4; -.
DR EnsemblMetazoa; XM_006564335; XP_006564398; LOC412865.
DR GeneID; 412865; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000005203; Linkage group LG11.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 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; IPR050149; Collagen_superfamily.
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; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_006564398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005203};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1173
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044659522"
FT DOMAIN 47..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 246..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..739
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 123060 MW; 939C356131953FD0 CRC64;
MRSRLQSLIF ALFCVTRVNA DFFAEKKEIN YDLIEAAVAS ADTDDTNLYI DDGLDGFPSF
GFRPGSEVKQ PYRLYLPEKL PAEFTLVATF KPMSFRTSYL FAVLNPFETV VQLGIRISDG
PGTNQNVSLI YTNSDLHSHS EEVAKFTVPK LSRKWSKIVI RVSTTDVTLY LNCHEMARQR
VTRIPLELVF DTASTLYIAQ AGPHIQEKYD GLLQSLKLYP GHPADLVKCT ADFNFDQDVD
LGSGEIDNEV IDNGSGFDIN LTDIGRDDDE DRSEESNPPP FITPPPPNPD YKGPKGEKGD
KGDKGESVRG PPGPPGPPGQ DEGPPGKKGE PGTCTCNATA LMASFTMPKM IQGPKGEQGV
PGQEGKQGQM GLTGVAGPPG ERGLEGPQGP KGDKGDVGIP GPEGPQGQKG EPGRDGIPGE
KGAQGPPGPP GKGEFSGYDP SWKPRGIYRT EGITMRPGLP GQKGEAGLPG SPGPKGETGI
AGAKGNKGEP GHKGAKGDHG NEGARGIQGS KGEPGAPGAP GLPGAPGENG RPAEKGDKGD
TGPEGKPGPP GAPGPPGLPG LSGPGGVNVG ESMLREKGDK GEGGARGYKG DKGTKGEKGD
KGDSGPAGIP GVNGIQGPQG NKGEPGKDGV AGVQGIAGAK GEKGERGPPG ATAIASSGDY
ITIKGEKGAE GKRGRRGRPG PPGPVGPPGK PGAMGEIGLP GWVGRPGTPG LPGPVGPAGP
KGEKGEPGTP SPYGVSVGVK GDKGDDGFPG IPGQPGREGQ RGPPGPPGPP GPPSQGNYIP
VPGPPGPPGP PGPPGLSLIG QKGEPGIGRS HIFGERDYYG VRQVQSVKKK HIPYPTLQGP
RTSLDELKAL RELKQLKELK EHLGAGTTAT RGPLESTTKI VPGAVTFQNT EAMTKMSAVS
PVGTLAYIID EQALLVRVNN GWQYIALGSL LPITTPAPPT TSPPPVNPPF EASNLINQIP
VKADGTGWYP RMLRMAALNE PFTGDMHGVR GADYACYRQA KRAGLRGTFR AFLSSRVQNV
DSIVRLGDRD LPIVNIKGDV LFNSWKEMFN GNGAYFSQNP RIYSFNGKNI LTDFAWPEKV
AWHGSHKLGD RAMDTYCDAW HSSSSDRYGL GSPLTGGRLL EQVRYSCDNK FALLCIEVTS
ETTRRRRNAE IAEDEDEMSE NDYKEYLDSL MED
//
