Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O35206

- COFA1_MOUSE

UniProt

O35206 - COFA1_MOUSE

Protein

Collagen alpha-1(XV) chain

Gene

Col15a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.
    Restin potently inhibits angiogenesis.

    GO - Molecular functioni

    1. structural molecule activity Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199055. Collagen degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XV) chain
    Cleaved into the following chain:
    Alternative name(s):
    Endostatin-XV
    Gene namesi
    Name:Col15a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:88449. Col15a1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. collagen trimer Source: UniProtKB-KW
    3. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 13671336Collagen alpha-1(XV) chainPRO_0000005790Add
    BLAST
    Chaini1177 – 1365189RestinPRO_0000005791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi673 – 6731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi792 – 7921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi799 – 7991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1216 ↔ 13561 Publication
    Disulfide bondi1318 ↔ 13481 Publication

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.By similarity
    O-glycosylated; contains chondroitin sulfate.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiO35206.
    PRIDEiO35206.

    PTM databases

    PhosphoSiteiO35206.

    Expressioni

    Tissue specificityi

    Detected in testis, brain, heart, kidney, skeletal muscle and skin (at protein level). Detected in heart and skeletal muscle.1 Publication

    Developmental stagei

    Detected at low levels from day 7 to 11 of embryonic development. Levels are much increased and remain high from day 15 to 17.

    Gene expression databases

    ArrayExpressiO35206.
    BgeeiO35206.
    CleanExiMM_COL15A1.
    GenevestigatoriO35206.

    Interactioni

    Subunit structurei

    Trimer; disulfide-linked.By similarity

    Protein-protein interaction databases

    IntActiO35206. 1 interaction.
    MINTiMINT-4104642.

    Structurei

    Secondary structure

    1
    1367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1197 – 12015
    Helixi1212 – 122211
    Beta strandi1229 – 12335
    Helixi1240 – 12423
    Helixi1246 – 12483
    Beta strandi1249 – 12513
    Beta strandi1261 – 12644
    Helixi1267 – 12704
    Beta strandi1271 – 12733
    Turni1291 – 12933
    Beta strandi1301 – 13033
    Helixi1318 – 13214
    Beta strandi1329 – 13346
    Helixi1335 – 13373
    Beta strandi1339 – 13413
    Beta strandi1344 – 13474
    Beta strandi1355 – 13584

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DY2X-ray2.00A1192-1367[»]
    ProteinModelPortaliO35206.
    SMRiO35206. Positions 1112-1165, 1194-1361.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO35206.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 249196Laminin G-likeAdd
    BLAST
    Domaini605 – 66561Collagen-like 1Add
    BLAST
    Domaini666 – 71752Collagen-like 2Add
    BLAST
    Domaini808 – 85043Collagen-like 3Add
    BLAST
    Domaini863 – 91250Collagen-like 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni229 – 604376Nonhelical region 1 (NC1)Add
    BLAST
    Regioni605 – 718114Triple-helical region 1 (COL1)Add
    BLAST
    Regioni719 – 74830Nonhelical region 2 (NC2)Add
    BLAST
    Regioni749 – 78335Triple-helical region 2 (COL2)Add
    BLAST
    Regioni784 – 80724Nonhelical region 3 (NC3)Add
    BLAST
    Regioni808 – 85245Triple-helical region 3 (COL3)Add
    BLAST
    Regioni853 – 86311Nonhelical region 4 (NC4)Add
    BLAST
    Regioni864 – 93471Triple-helical region 4 (COL4)Add
    BLAST
    Regioni935 – 96834Nonhelical region 5 (NC5)Add
    BLAST
    Regioni969 – 99830Triple-helical region 5 (COL5)Add
    BLAST
    Regioni999 – 103133Nonhelical region 6 (NC6)Add
    BLAST
    Regioni1032 – 108655Triple-helical region 6 (COL6)Add
    BLAST
    Regioni1087 – 109610Nonhelical region 7 (NC7)
    Regioni1097 – 111115Triple-helical region 7 (COL7)Add
    BLAST
    Regioni1112 – 1367256Nonhelical region 8 (NC8)Add
    BLAST

    Sequence similaritiesi

    Belongs to the multiplexin collagen family.Curated
    Contains 4 collagen-like domains.Curated
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00710000106713.
    HOGENOMiHOG000231591.
    HOVERGENiHBG080337.
    InParanoidiO35206.
    KOiK08135.
    OMAiPELITFH.
    PhylomeDBiO35206.
    TreeFamiTF315821.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    3.10.100.10. 1 hit.
    InterProiIPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR010515. Collagenase_NC10/endostatin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF01391. Collagen. 4 hits.
    PF06482. Endostatin. 2 hits.
    [Graphical view]
    SMARTiSM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF56436. SSF56436. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O35206-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHRRTAQGR RPRWLLSIIS ALLSAVLQTR AATGSASQVH LDLTVLIGVP     50
    LPSSVSFTTG YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAIGVAVKPN 100
    SAQGGVLFAI TDAFQKVIYL GLRLSSVEDG RQRVILYYTE PGSHVSREAA 150
    VFSVPVMTNR WNRFAVTVQG EEVALFMDCE EQSQVRFQRS SWPLTFEPSA 200
    GIFVGNAGAM GLERFTGSIQ QLTIYSDPRT PEELCEAQES SASGEASGFQ 250
    EMDEVAEIME AVTYTQAPPK ESHVDPISVP PTSSSPAEDS ELSGEPVPEG 300
    TPETNLSIIG HSSPEQGSGE ILNDTLEVHA MDGDPGTDDG SGDGALLNVT 350
    DGQGLSATAT GEASVPVTTV LEAENGSMPT GSPTLAMFTQ SIREVDTPDP 400
    ENLTTTASGD GEVPTSTDGD TEADSSPTGG PTLKPREEAT LGSHGEEWLT 450
    PAVSKMPLKA FEEEEASGTA IDSLDVIFTP TVVLEQVSRR PTDIQATFTP 500
    TVVLEETSGA PTDTQDALTP TVAPEQMFTA EPTDGGDLVA STEEAEEEGS 550
    GSMPPSGPPL PTPTVTPKRQ VTLVGVEAEG SGPVGGLDEG SGSGDIVGNE 600
    DLLRGPPGPP GPPGSPGIPG KPGTDVFMGP PGSPGEDGAP GEPGPQGPEG 650
    QPGLDGASGQ QGMKGEKGAR GPNGSAGEKG DPGNRGLPGP PGKNGEVGTP 700
    GVMGPPGPPG PPGPPGPGCT TELGFEIEGS GDVRLLSKPT ISGPTSPSGP 750
    KGEKGEQGAK GERGADGTST MGPPGPRGPP GHVEVLSSSL INITNGSMNF 800
    SDIPELMGPP GPDGVPGLPG FPGPRGPKGD TGVPGFPGLK GEQGEKGEPG 850
    AILTGDVPLE MMKGRKGEPG IHGAPGPMGP KGPPGHKGEF GLPGRPGRPG 900
    LNGLKGAKGD RGVTLPGPPG LPGPPGPPGP PGAVVNIKGA VFPIPARPHC 950
    KTPVGTAHPG DPELVTFHGV KGEKGSWGLP GSKGEKGDQG AQGPPGPPVD 1000
    PAYLRHFLNS LKGENEDASF RGESSNNLFV SGPPGLPGYP GLVGQKGEAV 1050
    VGPQGPPGIP GLPGPPGFGR PGVPGPPGPP GPPGPPAILG AAVALPGPPG 1100
    PPGQPGLPGS RNLVTALSDM GDMLQKAHLV IEGTFIYLRD SGEFFIRVRD 1150
    GWKKLQLGEL IPIPADSPPP PALSSNPYQP QPPLNPILSA NYERPVLHLV 1200
    ALNTPVAGDI RADFQCFQQA RAAGLLSTFR AFLSSHLQDL STVVRKAERF 1250
    GLPIVNLKGQ VLFNNWDSIF SGDGGQFNTH IPIYSFDGRD VMTDPSWPQK 1300
    VVWHGSNPHG VRLVDKYCEA WRTTDMAVTG FASPLSTGKI LDQKAYSCAN 1350
    RLIVLCIENS FMTDTRK 1367
    Length:1,367
    Mass (Da):140,472
    Last modified:April 3, 2007 - v2
    Checksum:iBD92E26B5E99B607
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti380 – 3801T → L in AAC53387. (PubMed:9339358)Curated
    Sequence conflicti499 – 4991T → K in BAE21987. (PubMed:16141072)Curated
    Sequence conflicti569 – 5691R → K in AAG27545. (PubMed:11068203)Curated
    Sequence conflicti593 – 5931S → A in AAG27545. (PubMed:11068203)Curated
    Sequence conflicti699 – 6991T → P in AAC53387. (PubMed:9339358)Curated
    Sequence conflicti699 – 6991T → P in AAG27545. (PubMed:11068203)Curated
    Sequence conflicti736 – 7361L → M in AAG27545. (PubMed:11068203)Curated
    Sequence conflicti779 – 7791P → R in AAC53387. (PubMed:9339358)Curated
    Sequence conflicti1116 – 11161A → G in AAC53387. (PubMed:9339358)Curated
    Sequence conflicti1116 – 11161A → G in AAG27545. (PubMed:11068203)Curated
    Sequence conflicti1309 – 13091H → Y in AAG27545. (PubMed:11068203)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011450 mRNA. Translation: AAC53387.1.
    AF261131
    , AF261109, AF261110, AF261111, AF261112, AF261113, AF261114, AF261115, AF261116, AF261117, AF261118, AF261119, AF261120, AF261121, AF261122, AF261123, AF261124, AF261125, AF261126, AF261127, AF261128, AF261129, AF261130 Genomic DNA. Translation: AAG27545.1.
    AK134030 mRNA. Translation: BAE21987.1.
    AL772232, AL928652 Genomic DNA. Translation: CAM13891.1.
    AL928652, AL772232 Genomic DNA. Translation: CAM20188.1.
    CCDSiCCDS18159.1.
    RefSeqiNP_034058.2. NM_009928.3.
    UniGeneiMm.233547.

    Genome annotation databases

    EnsembliENSMUST00000102917; ENSMUSP00000099981; ENSMUSG00000028339.
    GeneIDi12819.
    KEGGimmu:12819.
    UCSCiuc008sum.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011450 mRNA. Translation: AAC53387.1 .
    AF261131
    , AF261109 , AF261110 , AF261111 , AF261112 , AF261113 , AF261114 , AF261115 , AF261116 , AF261117 , AF261118 , AF261119 , AF261120 , AF261121 , AF261122 , AF261123 , AF261124 , AF261125 , AF261126 , AF261127 , AF261128 , AF261129 , AF261130 Genomic DNA. Translation: AAG27545.1 .
    AK134030 mRNA. Translation: BAE21987.1 .
    AL772232 , AL928652 Genomic DNA. Translation: CAM13891.1 .
    AL928652 , AL772232 Genomic DNA. Translation: CAM20188.1 .
    CCDSi CCDS18159.1.
    RefSeqi NP_034058.2. NM_009928.3.
    UniGenei Mm.233547.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DY2 X-ray 2.00 A 1192-1367 [» ]
    ProteinModelPortali O35206.
    SMRi O35206. Positions 1112-1165, 1194-1361.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O35206. 1 interaction.
    MINTi MINT-4104642.

    PTM databases

    PhosphoSitei O35206.

    Proteomic databases

    PaxDbi O35206.
    PRIDEi O35206.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102917 ; ENSMUSP00000099981 ; ENSMUSG00000028339 .
    GeneIDi 12819.
    KEGGi mmu:12819.
    UCSCi uc008sum.1. mouse.

    Organism-specific databases

    CTDi 1306.
    MGIi MGI:88449. Col15a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00710000106713.
    HOGENOMi HOG000231591.
    HOVERGENi HBG080337.
    InParanoidi O35206.
    KOi K08135.
    OMAi PELITFH.
    PhylomeDBi O35206.
    TreeFami TF315821.

    Enzyme and pathway databases

    Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei O35206.
    NextBioi 282290.
    PROi O35206.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35206.
    Bgeei O35206.
    CleanExi MM_COL15A1.
    Genevestigatori O35206.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    3.10.100.10. 1 hit.
    InterProi IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR010515. Collagenase_NC10/endostatin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF01391. Collagen. 4 hits.
    PF06482. Endostatin. 2 hits.
    [Graphical view ]
    SMARTi SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF56436. SSF56436. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of mouse type XV collagen sequences and mapping of the corresponding gene to 4B1-3. Comparison of mouse and human alpha 1 (XV) collagen sequences indicates divergence in the number of small collagenous domains."
      Haegg P.M., Horelli-Kuitunen N., Eklund L., Palotie A., Pihlajaniemi T.
      Genomics 45:31-41(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: 129/Sv.
      Tissue: Kidney.
    2. "Structure of the mouse type XV collagen gene, Col15a1, comparison with the human COL15A1 gene and functional analysis of the promoters of both genes."
      Eklund L., Muona A., Lietard J., Pihlajaniemi T.
      Matrix Biol. 19:489-500(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Thymus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity."
      Sasaki T., Larsson H., Tisi D., Claesson-Welsh L., Hohenester E., Timpl R.
      J. Mol. Biol. 301:1179-1190(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: FUNCTION.
    7. "Crystal structure of the angiogenesis inhibitor endostatin at 1.5-A resolution."
      Hohenester E., Sasaki T., Olsen B.R., Timpl R.
      EMBO J. 17:1656-1664(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1192-1367, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCOFA1_MOUSE
    AccessioniPrimary (citable) accession number: O35206
    Secondary accession number(s): A2AJY3, Q3UZ71, Q9EQD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    The name Restin has also been used for CAP-Gly domain-containing linker protein 1 the product of the CLIP1 gene.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3