ID A0A7J7W2B1_PIPKU Unreviewed; 1434 AA.
AC A0A7J7W2B1;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN ORFNames=mPipKuh1_003088 {ECO:0000313|EMBL:KAF6331595.1};
OS Pipistrellus kuhlii (Kuhl's pipistrelle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Pipistrellus.
OX NCBI_TaxID=59472 {ECO:0000313|EMBL:KAF6331595.1, ECO:0000313|Proteomes:UP000558488};
RN [1] {ECO:0000313|EMBL:KAF6331595.1, ECO:0000313|Proteomes:UP000558488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPipKuh1 {ECO:0000313|EMBL:KAF6331595.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6331595.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC {ECO:0000256|ARBA:ARBA00058706}.
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00058695}.
CC -!- SUBUNIT: Interacts moderately with EFEMP2.
CC {ECO:0000256|ARBA:ARBA00065596}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00061770}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6331595.1}.
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DR EMBL; JACAGB010000012; KAF6331595.1; -; Genomic_DNA.
DR Proteomes; UP000558488; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 1.
DR FunFam; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 1.
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; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
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, ECO:0000313|EMBL:KAF6331595.1};
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:UP000558488};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 106..294
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 155..293
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..644
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..723
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..888
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..964
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 148027 MW; 95DA22288ED26F10 CRC64;
MTRERRALSP WSCSGRDRRE GGEGAASALP DGAGTPGFSR RKRARPPVAS AELGRLLSAS
GAGQSREMEP RRNERRWFLP RLLWVSALLS AADRTRAETA PPSQAHLDLM EIIGLPLSPS
VSFVTGYGGF PAYSFGPGAN VGRPASVLLP PAFFRDFAIS VTVKPGSDRG GVLFAVTDTF
QTVVHLGLQL SAVADGQQRV ILYYTEPGSA VSQEAAAFSV PVMTHRWNRF DVIVEGEEVT
LVLDCEEHSR VPFQRSSRAL VFEPRAGIFV GSAGAKQLEK FIGSIQQLTI HPDPRAPEKR
CEVEESSASG EASGLQETDG VAEILDADTY TQAPPKESKV EPINTPPTPT FPSKDSELSR
EPVPEGTLKT PNLSAILNSS AEQGSGDILN DTLEEVHTMN RVPITDPGSG DGAFLHVTGE
SPHTVEDLAT TVATREANVT IDTAWEAEVT FSTAGEANVT VSTAEEAEEG RVPTGDPTLS
MPTVEPGEGA TPSPETEEGS AEISGEEAEM PTSTDGDAQA STVATGEPAL FMSTQEPEEG
GPVSEGSLTT AAEMPLSTCE DEEEEEARKV PTSGPPPGTR TAAPEQAVTF GPSEDDLAAA
TTEEPLSGAG AEEPGSVPPE GRPLPIPTVT PATAVPPVTA SVGAEAEGSG LGWDPEVGSG
SGDLGPSEEL LRGPPGPPGP PGLPGTPGKP GTDVFMGPPG SPGEDGAAGE PGPRGPRGQP
GLDGASGRPG TKGEKGARGP NGSVGEKGDP GNRGSPGPPG KNGQVGIMGP PGPPGPPGPP
GPECTMEPEF EYIEGSGNIR PRQEPRISGP NGLKGEKGDP GIKGERGMDG ASIVGPPGPR
GPPGRIEVLP SSLINMTHGS MNLSDIPELA GPPGPDGMPG LPGFPGPRGP KGDTGVPGFP
GLKGEQGEKG EAGAILSGDV PLERLRGEKG EPGAHGAPGP MGPKGPPGHK GEFGLPGRPG
RPGLNGFKGA KGDRGVMMPG PPGLPGPPGP PGPPGAVINI KGAVFPIPTR PHCKMPVGAA
HPGNSELITF HGVKGEKGTW GLPGSKGEKG DQGAQGPPGP PMDPAYLRHF INSMKGENGD
RGFKGEKGDS ISDFSVSGPP GRPGSPGQAG QKGEAIVGPQ GPPGVPGLPG PPGYGRPGSP
GPPGPPGPPG PPAILGAAVA LPGPPGPPGQ PGLPGSRNLV TALSSMADML QYAHLVTEGT
FIYLRDSTEF FIRVRNGWKK LQLGELIPIP ADSPPPPALS SNNPHPLRPP LMPVSSVNYG
KPELHLIALN MPFSGDIRAD FQCFQQARDA GLLSTYRAFL STHLQDLSTI VRKAERYSLP
IVNLKGQVLF NNWDSIFSGH GGQFSTHVPI YSFDGRDVMT DPSWPQKVVW HGSNPHGVRL
EDQYCEAWRT ASTAVTGLAS PLSTGKILDQ KAYSCSSRLI VLCIENSFLT DARK
//
