ID A0A2R9BLV4_PANPA Unreviewed; 2521 AA.
AC A0A2R9BLV4;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Collagen type VI alpha 3 chain {ECO:0008006|Google:ProtNLM};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000030674.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000030674.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AJFE02041782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02041783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPPAT00000053537.1; ENSPPAP00000030674.1; ENSPPAG00000038270.1.
DR GeneTree; ENSGT00940000156462; -.
DR OMA; KGGRQAN; -.
DR Proteomes; UP000240080; Unplaced.
DR Bgee; ENSPPAG00000038270; Expressed in heart and 5 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd22629; Kunitz_collagen_alpha3_VI; 1.
DR CDD; cd01481; vWA_collagen_alpha3-VI-like; 3.
DR CDD; cd01450; vWFA_subfamily_ECM; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 9.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR041900; vWA_collagen_alpha3-VI-like.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24020:SF13; COLLAGEN ALPHA-3(VI) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 9.
DR PRINTS; PR00759; BASICPTASE.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 9.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53300; vWA-like; 9.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50234; VWFA; 9.
PE 4: Predicted;
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..208
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 225..397
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 417..593
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 621..792
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 824..997
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1027..1200
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1226..1412
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1752..1931
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1969..2165
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 2335..2429
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2456..2506
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 1000..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2209..2238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2302..2330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2417..2437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2521 AA; 273318 MW; 736559A6F550BDC9 CRC64;
TGVCPHARLI FVFLVVMGFP LVGQAVVEVN KRDIVFLVDG SSALGLANFN AIRDFIAKVI
QRLEIGQDLI QVAVAQYADT VRPEFYFNTH PTKREVITAV RKMKPLDGSA LYTGSALDFV
RNNLFTSSAG YRAAEGIPKL LVLITGGKSL DEISQPAQEL KRSSIMAFAI GNKGADQAEL
EEIAFDSSLV FIPAEFRAAP LQGMLPGLLA PLRTLSGTPE ESKRDILFLF DGSANLVGQF
PVVRDFLYKI IDELNVKPEG TRIAVAQYSD DVKVESRFDE HQSKPEILNL VKRMKIKTGK
ALNLGYALDY AQRYIFVKSA GSRIEDGVLQ FLVLLVAGRS SDRVDGPASN LKQSGVVPFI
FQAKNADPAE LEQIVLSPAF ILAAESLPKI GDLQPQIVNL LKSVHNGAPA PVSGEKDVVF
LLDGSEGVRS GFPLLKEFVQ RVVESLDVGQ DRVRVAVVQY SDRTRPEFYL NSYMNQQDVV
NAVRQLTLLG GPTPNTGAAL EFVLRNILVS SAGSRITEGV PQLLIVLTAD RSGDDVRNPS
VVVKRGGAVP IGIGIGNADI TEMQTISFIP DFAVAIPTFR QLGTVQQVIS ERVTQLTREE
LSRLQPVLQP LPSPGVGGKR DVVFLIDGSQ SAGPEFQYIR TLIERLVDYL DVGFDTTRVA
VIQFSDDPKV EFLLNAHSSK DEVQNAVQRL RPKGGRQINV GSALEYVSRN IFKRPLGSRI
EEGVPQFLVL ISSGKSDDEV DDPAVELKQF GVAPFTIARN ADQEELVKIS LSPEYVFSVS
TFRELPSLEQ KLLTPITTLT SEQIQKLLAS TRYPPPAVES DAADIVFLID SSEGVRPDGF
AHIRDFVSRI VRRLNIGPSK VRVGVVQFSN DVFPEFYLKT YRSQAPVLDA IRRLRLRGGS
PLNTGKALEF VARNLFVKSA GSRIEDGVPQ HLVLVLGGKS QDDVSRFAQV IRSSGIVSLG
VGDRNIDRTE LQTITNDPRL VFTVREFREL PNIEERIMNS FGPSAATPAP PGVDTPPPSR
PEKKKADIVF LLDGSINFRR DSFQEVLRFV SEIVDTVYED GDSIQVGLVQ YNSDPTDEFF
LKDFSTKRQI IDAINKVVYK GGRHANTKVG LEHLRVNHFV PEAGSRLDQR VPQIAFVITG
GKSVEDAQDV SLALTQRGVK VFAVGVRNID SEEVGKIASN SATAFRVGNV QELSELSEQV
LETLHDAMHE TLCPGVTDAA KACNLDVILG FDGSRDQNVF VAQKGFESKV DAILNRISQM
HRVSCSGGRS PTVRVSVVAN TPSGPVEAFD FDEYQPEMLE KFRNMRSQHP YVLTEDTLKV
YLNKFRQSSP DSVKVVIHFT DGADGDLADL HRASENLRQE GVRALILVGL ERVAHLERLM
HLEFGRGFMY DRPLRLNLLD LDYELAEQLD NIAEKACCGV PCKCSGQRGD RGPIGSIGPK
GIPGEDGYRG YPGDEGGPGE RGPPGVNGTQ GFQGCPGQRG VKGSRGFPGE KGEVGEIGLD
GLDGEDGDKG LPGSSGEKGN PGRRGDKGPR GEKGERGDVG IRGDPGNPGQ DSQERGPKGE
TGDLGPMGVP GRDGVPGGPG ETGKNVSAIR ALGGSGNKGG PGQPGFEGEQ GTRGAQGPAG
PAGPPGLIGE QGISGPRVSL GHIAKQAEKP GPKGGIGNRG PRGETGDDGR DGVGSEGRRG
KKGNPGEPGL NGTTGPKGIR GRRGNSGPPG IVGQKGDPGY PGPAVSIYPQ CALIQSIKDK
CRPLECPVFP TELAFALDTS EGVNQDTFGR MRDVVLSIVN DLTIAESNCP RGARVAVVTY
NNEVTTEIRF ADSKRKSVLL DKIKNLQVAL TSKQQSLETA MSFVARNTFK RVRNGFLMRK
VAVFFSNTPT RASPQLREAV LKLSDAGITP LFLTRQEDRQ LINALQINNT AVGHALVLPA
GRDLTDFLEN VLTCHVCLDV CNIDPSCGFG SWRPSFRDRR AAGSDVDIDM AFILDSAETT
TLFQFNEMKK YIAYLVRQLD MSPDPKASQH FARVAIVQHA PSESVDNASM PPVKVEFSLT
DYGSKEKLVD FLSRGMTQLQ GTRALGSAIE YTIENVFESA PNPRDLKIVV LMLTGKVPEQ
QLEEAQRVIL QAKCKGYFFV VLGIGRKVNI KEVYTFASEP NDVFFKLVDK STELNEEPLM
RFGRLLPSFV SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK FGHKQVNVPN NVTSSPTSNP
VTTMKPVTTT KPPVTTTTKP VTIINQPSVK PAAAKPAPAK PVAAKPVATK TATVRPPVAV
RPAMAAKPVA AKPAAVRPPA AAAAKPVATK PEVPRPQAAK PAATKPATTK PVVKMSREVQ
VFEITENSAK LHWERPEPPG PYFYDLTVTS AHDQSLVLKQ NLTVTDRVIG GLLAGQTYHV
AVVCYLRSQV RATYHGSFST KKSQPPPPQP ARSASSSTIN LMVSTEPLAL TETDICKLPK
DEGTCRDFIL KWYYDPNTKS CARFWYGGCG GNENKFGSQK ECEKVCAPVL AKPGVISVMG
T
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