ALBU_PETMA
ID ALBU_PETMA Reviewed; 1423 AA.
AC Q91274;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Serum albumin SDS-1;
DE Flags: Precursor;
GN Name=SDS-1;
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1304910; DOI=10.1002/pro.5560010211;
RA Doolittle R.F., Gray J.E.;
RT "Characterization, primary structure, and evolution of lamprey plasma
RT albumin.";
RL Protein Sci. 1:289-302(1992).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=11079379; DOI=10.1016/s0305-0491(00)00265-0;
RA Danis M.H., Filosa M.F., Youson J.H.;
RT "An albumin-like protein in the serum of non-parasitic brook lamprey
RT (Lampetra appendix) is restricted to preadult phases of the life cycle in
RT contrast to the parasitic species Petromyzon marinus.";
RL Comp. Biochem. Physiol. 127B:251-260(2000).
CC -!- FUNCTION: Serum albumin, the main protein of plasma, has a good binding
CC capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones,
CC bilirubin and drugs. Its main function is the regulation of the
CC colloidal osmotic pressure of blood.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- DEVELOPMENTAL STAGE: Adults. {ECO:0000269|PubMed:11079379}.
CC -!- MISCELLANEOUS: In the sea lamprey, there are two forms of albumin, AS
CC and SDS-1.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; M74193; AAA49271.1; -; mRNA.
DR PIR; S27941; S27941.
DR AlphaFoldDB; Q91274; -.
DR SMR; Q91274; -.
DR PRIDE; Q91274; -.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00015; ALBUMIN; 6.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR020857; Serum_albumin_CS.
DR InterPro; IPR014760; Serum_albumin_N.
DR PANTHER; PTHR11385; PTHR11385; 6.
DR Pfam; PF00273; Serum_albumin; 8.
DR PRINTS; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 7.
DR SUPFAM; SSF48552; SSF48552; 7.
DR PROSITE; PS00212; ALBUMIN_1; 7.
DR PROSITE; PS51438; ALBUMIN_2; 7.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Copper; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Lipid-binding; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..29
FT /id="PRO_0000001093"
FT CHAIN 30..1423
FT /note="Serum albumin SDS-1"
FT /id="PRO_0000001094"
FT DOMAIN 29..230
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 231..426
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 427..608
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 609..811
FT /note="Albumin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 812..1031
FT /note="Albumin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT REPEAT 913..916
FT /note="2-1"
FT REPEAT 917..920
FT /note="2-2"
FT REPEAT 921..924
FT /note="2-3"
FT REPEAT 925..928
FT /note="2-4"
FT REPEAT 929..932
FT /note="2-5"
FT REPEAT 933..935
FT /note="2-6"
FT REPEAT 936..939
FT /note="2-7"
FT DOMAIN 1032..1226
FT /note="Albumin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 1227..1422
FT /note="Albumin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT REGION 910..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..939
FT /note="7 X 4 AA tandem repeats of S-T-T-T"
FT BINDING 36
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 87..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 109..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 124..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 167..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 211..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 244..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 289..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 311..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 326..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 363..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 407..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 439..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 484..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 506..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 521..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 556..601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 622..668
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 667..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 689..705
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 704..715
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 747..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 791..802
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 825..871
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 870..879
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 892..907
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 906..947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 969..1014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1013..1022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1045..1091
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1090..1099
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1112..1128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1127..1138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1163..1208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1207..1216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1239..1285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1284..1291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1304..1320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1319..1330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1359..1404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 1403..1412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 1423 AA; 159094 MW; 22F3E6950CCE9318 CRC64;
MGKAMLKLCI TLMVLVFSGT AESKGVMRRE DESFPHLKSR LCGGLNGLGE DAYRSHCVVY
YTKRMGVVSL DHVEELANHC LRIVKQCCAE GAADDCLQTE LAAVQEQVCT RMSEAKDVPL
VGRCCALAGS ERHDCFHHAG GVAEGEGAWP HALPVTSPPE YDSVTVCALH ATANARLYDT
LLWEFSRRYP SASDSHLIAL ANEFITGLTT CCLVEEEHGA CLATLREDFK HKLTEASHKS
QNLCKALKSL GKEKFEDRII VRFTQRAPQA PFELIQKLAH RFEVLAEKCC ELGHSDRCLV
EERYTVDDEL CLEQSFVATC PRLSSCCSLS GSSRAQCLET VPVLETSDKA SPATPTLPIS
EQCTLWAGKP VEFHKRVVWQ ISHRYPTTGV AQVEALAHHY LEHLTICCAS EDKDTCIATE
VAEFKSEVEK VHTKSDWWCR MSDLLGTDRF NLLLIVTYSQ RVPQATFEQV EEISHHFALI
TRKCCSHRKN GSCFLEERYA LHDAICRDEA WLSGLAEVSR CCAMDGRARI LCFDELSSHL
NASVEERPEL CSTSLCSKYH DLGFEFKQRV AYGFGQRFPK AAMGQMRDLI SKYLAMVQRC
CDAMSDFKMD VEEVELRAHR LCLDAHQLGE EKLADRIMIG LAQRISVASF VNISSVALHF
AQSVIKCCDA DHEKTCFMEQ EFALEDQVCS DSEALSHIPS VSRCCELHPF DRSVCFHSLR
STQASTLAST HVAVGKDDSL PGHVEECQAF ASGNHSLTDQ VMFEFARRHP RASVSQVESL
ARLYSELARA CCALTDADQE SCLHTARSQA RQEALKSLQR SERICNTLSA IGKEKFEDRI
VIALSQKATD ASFEQILEIA NRMSRGLARC CEQGNNVGCL MDHRHALHEA ICSTPDGSLP
QSVAACCNTS NTSTTTSTTT STTTSTTTST TTSTTSTTTA AEIRDSCFDN LQANVSRAHA
PFYSNSQLCL MKLRTPHRFL ERFLWEFGRR HPQAALSQVE ELAEMYVKMT DSCCGKLHSK
SCFTEQRHTI HMEIRHAYAE VQHICGSLHS RGEETFIQRE VTLLSQKAPN ASFEKVSQLA
RHFLSLAKKC CAPDHAAGCF LEEPYAIHDE VCRDDEVVDQ VGGLATCCRM SGTSRAKCLA
QLPRDLGRHG NRETPEFDEL KICELRRDNP AVLMEKILYE FGRRHSDSAV SEVKNFAQKF
SHSVTECCTS EKTHECFVEK RAAIEKVIKD EEAKGNLTCQ RLKAQGVEHF EQLVILNFAR
AAKSLPMEKV VEFAHRFTRI AGQCCEHDTH CLIDESFHLH AEMCGDHGYI MAHPGVANCC
KSDVSEQGTC FKIHEDVHHA EEILSKDVSP AHPTAERVCL RYRQFPEKFI NLALFELVHR
LPLLESSVLR RKALAYTGFT DDCCRAVDKT ACFTEKLEAI KSS
