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Database: UniProt
Entry: F1S285_PIG
LinkDB: F1S285_PIG
Original site: F1S285_PIG 
ID   F1S285_PIG              Unreviewed;      1760 AA.
AC   F1S285;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Collagen type XIV alpha 1 chain {ECO:0000313|Ensembl:ENSSSCP00000006405.3};
GN   Name=COL14A1 {ECO:0000313|Ensembl:ENSSSCP00000006405.3,
GN   ECO:0000313|VGNC:VGNC:97936};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000006405.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000006405.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000006405.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000006405.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   PeptideAtlas; F1S285; -.
DR   Ensembl; ENSSSCT00000006580.5; ENSSSCP00000006405.3; ENSSSCG00000005997.6.
DR   VGNC; VGNC:97936; COL14A1.
DR   GeneTree; ENSGT00940000153769; -.
DR   HOGENOM; CLU_002527_2_0_1; -.
DR   OMA; REMQSDX; -.
DR   TreeFam; TF329914; -.
DR   ChiTaRS; COL14A1; pig.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Bgee; ENSSSCG00000005997; Expressed in ovary and 40 other cell types or tissues.
DR   ExpressionAtlas; F1S285; baseline and differential.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 7.
DR   CDD; cd01482; vWA_collagen_alphaI-XII-like; 2.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24020:SF15; COLLAGEN ALPHA-1(XIV) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   Pfam; PF00041; fn3; 8.
DR   Pfam; PF00092; VWA; 2.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00327; VWA; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 7.
DR   SUPFAM; SSF53300; vWA-like; 2.
DR   PROSITE; PS50853; FN3; 7.
DR   PROSITE; PS50234; VWFA; 2.
PE   1: Evidence at protein level;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1S285};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          32..123
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          158..330
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          355..444
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          445..536
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          537..626
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          627..716
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          717..810
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          811..901
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1012..1185
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          126..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1442..1591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1626..1760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1555
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1638..1655
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1690..1727
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1760 AA;  189820 MW;  68FD7CABBE22A6FB CRC64;
     MKIFQCKMQY WLFPAFLAVT YFCTIVQGQV APPTRLRYNV LSHDSIQISW KAPRGKFGGY
     KLLVTPAAGG KTNQLNLQNT ATKAIIQGLM PDQNYTVQII AYHKDKESKP AQGQFRIKDI
     EKRKEPKPRV KVVDRDGNKP STPEEEVKFF CQTPAIADIV ILVDGSWSIG RFNFRLVRSF
     LENLVTAFNV GSEKTRIGLA QYSGDPRIEW HLNAFSTKDE VIEAVRNLPY KGGNTLTGLA
     LNYIFENSFK PEAGARTGVS KIGILITDGK SQDDVIPPSR NLRESGVELF AIGVKNADEN
     ELREIASEPD NTHVYNVAEF DLMHTVVESL TRTVCSRVEE QDREIKASAL AAIGPPTELL
     TSEVTARSFM VNWTHAPGKV EKYRVVYYPT RGGKPEEVVV DGSISSTVLK NLMSLTEYQI
     AVFAIYAHTA SEGLRGTETT LALPIASDLE LYDVTENSLR ARWNPVAGAS GYLILYAPLT
     EGLAGDEKEM KIGETHTDIE LRGLLPNTEY TVTVYAMFGE EASDPVTGQE TTLPLSPPRN
     LRISNVGSNS ARLAWDPTSR RISGYRIVYN NADGTEINEV EVDPITTFPL KGLTPITEYT
     VAIFSIYDEG QSEPLTGIFS TEEVPAQQYL EIDEVMTDSF RVTWHPLSAD EGQHKLMWIP
     VYGGKTQEVV LKEDQDSYVI EGLEPGTEYE VSLLAVLDDG SESEVVTAVG TTLFRTGIRN
     LVVDDETTSS LRVKWDISDS SVQQFRVTYL TAQGDPAEEV VGTVMVSGNQ NDLLLKNLLS
     NTEYKVTVTP IYDDGEGVSV SAPGKTLPPS GPQNLRVSEE WYNRLRITWD PPSSPVKGYR
     IVYKPVSVAG PTLETFVGAN INTILITNLL SGMDYNVKIF ASQASGFSDA LTGVVKTLFL
     GVTDLQADQI QMTSLCARWQ VQRHATAYRI VIESLQDTQK QESTLGGGTT RHCFYGLQPD
     SQYKISVYTK LQEMEGPSVS IMEKTKSLPT PPPTFPPTIP PAKEVCKAAK ADLVFMVDGS
     WSIGDENFNK ITNFLYSTVG ALDKIGADGT QVAMVQFTDD PRTEFKLNTY KTKETLLDAI
     KHISYKGGNT KTGKAIKHVR DNLFTAESGI RRGIPKVIVV ITDGRSQDDV NKISKEMQLD
     GYSIFAVGVA DADYSELVSI GSKPSARHVF FVDDFDAFKK IEDELITFVC ETASATCPLV
     HKDGIDLAGF KMMELFGLVE KDFSSVEGVS MEPGTFNVYP CYHLHKDALV SQPTKYLHPE
     GLPSDYTISF LFRVLPDTPE EPFALWEILN KNSDPLVGVI LDNGGKTLTY FNYDYSGDFQ
     TVTFEGPEIR KIFYGSFHKL HIIVSKTMAK VVIDCKEVGE KAINASSNIT SDGVEVLGRM
     VRSRGPNGNS APFQLQMFDI VCSTSWANKD KCCELPGLRD EETCPELPHS CSCSEINKGA
     LGPAGPPGGP GLRGPKGQRG EPGPKGPDGP RGETGPPGHQ GPPGPQGPSG LSIQGMPGMP
     GEKGEKGETG LPGPQGIPGS VGSPGRDGSP GQRGFPGKDG SSGPPGPPGP IGIPGAPGVP
     GITGSMGPQG ALGPPGAPGA KGERGERGDL QSQAMVRAVA RQVCEQLIQS HMARYTAILN
     QIPSHSSSIR TIQGPPGEPG RPGSPGAPGE QGPPGSPGFP GNAGVPGTPG ERGLTGVKGE
     KGNPGIGTQG PRGPPGPAGP SGESRPGSPG PPGSPGPRGP PGHLGVPGPQ GPSGQPGYCD
     PSSCSAYGVG DLIPYNDYQH
//
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