ID A0A7M7LRJ9_APIME Unreviewed; 1163 AA.
AC A0A7M7LRJ9; A0A8B6Z1C2;
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 X5 {ECO:0000313|RefSeq:XP_006564401.1};
GN Name=LOC412865 {ECO:0000313|RefSeq:XP_006564401.1};
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_006564401};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_006564401}
RP IDENTIFICATION.
RC STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:XP_006564401};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_006564401.1}
RP IDENTIFICATION.
RC STRAIN=DH4 {ECO:0000313|RefSeq:XP_006564401.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_006564401.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
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DR RefSeq; XP_006564401.1; XM_006564338.3.
DR AlphaFoldDB; A0A7M7LRJ9; -.
DR EnsemblMetazoa; XM_006564338; XP_006564401; 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_006564401.1};
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..1163
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044660354"
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..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1163
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 476..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..548
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..729
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..763
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..784
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 121818 MW; 368ADC5538741534 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 GKGEFSGYDT 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
//
